Seeing Further: The Story of Science, Discovery, and the Genius of the Royal Society - Bill Bryson (2010)
11. GEORGINA FERRY
X-RAY VISIONS: STRUCTURAL BIOLOGISTS AND SOCIAL ACTION IN THE TWENTIETH CENTURY
Georgina Ferry is a science writer, broadcaster and biographer. She is the author of Dorothy Hodgkin: A Life, The Common Thread: A Story of Science, Politics, Ethics and the Human Genome (with John Sulston), A Computer Called LEO: Lyons Teashops and the World’s First Office Computer, and most recently, Max Perutz and the Secret of Life.
SCIENTISTS NEED TENACITY: NONE MORE SO THAN THOSE WHOSE PAINSTAKING, DRAWN-OUT WORK PICTURED THE THREE-DIMENSIONAL STRUCTURES OF THE VAST MOLECULES BUILT BY LIVING CELLS. AS GEORGINA FERRY RELATES, THE STRENGTH OF CHARACTER DEMANDED BY CRYSTALLOGRAPHY OFTEN WENT ALONG WITH STRONG CONVICTIONS ABOUT THE ROLE OF SCIENCE IN SOCIETY.
Anyone crossing the courtyard of Burlington House in Piccadilly on a certain day in 1945 would have seen a contrasting couple sitting on the steps of the East Wing, then home to the Royal Society. She was slight, girlish, a fair-haired woman in her thirties with penetrating blue eyes. He was a decade older, shock-headed, fleshy-faced and physically imposing. Waiting for a colleague, they were discussing her latest scientific result. Delightedly she confided that after two years of wartime work, still officially a secret, she and her colleagues had solved the structure of penicillin. ‘You’ll get the Nobel Prize for this,’ he said. She countered that she would far rather be elected one of the Fellows on whose doorstep she was sitting. Without irony, he told her ‘That’s more difficult.’ 1
Wrapped up in this anecdote about Dorothy Crowfoot Hodgkin and John Desmond Bernal is a whole chapter of interlocking stories: about collegiality, about scientific workers of both sexes, about the impact of war on research, but above all about the conviction that knowing how biological molecules were constructed from atoms in three dimensions would fundamentally alter our understanding of life. Hodgkin (FRS 1947) and Bernal (FRS 1937), her former PhD supervisor and lifelong mentor, were among the founders of a project that at first seemed hopeless, even quixotic in its ambition: to use physical techniques to reveal the structure of life in atomic detail. Today their inheritors are at work every day, using essentially the same techniques to build a catalogue of the shapes of every molecule in the living body, and applying that information to understand health and disease and to design new drugs.
The legacy of the structure pioneers, however, is richer than the sum of their scientific achievements. Each in his or her own way, they gave their considerable energies to causes such as scientific education, the organisation of research, international understanding, gender equality, human rights, prison reform and world peace. Partly because the subject crossed so many disciplinary boundaries, but also because of the personalities involved, they also developed a way of doing science that valued collaboration over competition, and fostered egalitarianism in relation to rank, gender and class.
FATHER AND SON
Everyone in this story can trace a scientific lineage back to William Henry Bragg (FRS 1907) or his son William Lawrence Bragg (FRS 1921).2
Most would also credit the Braggs with establishing the egalitarian outlook that the early structural biologists shared. William H. Bragg was born in the UK and studied at Cambridge, but in 1885, at the age of twenty-three, he was appointed to the professorship in physics at the University of Adelaide. In 1909 he returned from Australia to take up the chair in physics at Leeds. His nineteen-year-old son Willie immediately went to Cambridge to study natural sciences.
In 1912 the Munich-based physicist Max von Laue and his junior colleagues reported that a zinc sulphide crystal could diffract a beam of X-rays, producing a characteristic pattern of spots on a photographic plate and demonstrating the wave-like nature of X-radiation. Bragg père, who at that time inclined to the view that X-rays consisted of particles, was tipped off about the paper by a colleague who was working in Germany. When Willie came home for the long vacation they pored over the problem, and in subsequent months began their own experiments. Willie confirmed that X-rays formed diffraction patterns on passing through crystals (in the same way that light does on passing through narrow slits), and therefore behaved like waves. He went on to demonstrate that a simple mathematical formula (now known as Bragg’s Law) could relate the positions and intensities of the spots in the pattern to the positions of the parallel layers of atoms in the crystal from which the X-rays were reflected. The formula required a figure for the wavelength of the X-rays, and the Braggs were able to measure this using an X-ray spectrometer of Bragg senior’s invention. Applying the formula to X-ray photographs of simple compounds such as sodium chloride, Willie Bragg was able to draw a picture of the sodium and chlorine atoms neatly alternating throughout the cubic lattice, like the simplest of wallpaper patterns but in three dimensions.
The Braggs had turned X-ray diffraction from an intriguing observation into a tool for exploring what matter is made of in the range that was too small to be seen with a microscope, and too large for chemical analysis. They shared the 1915 Nobel Prize in physics for their discovery. The announcement came when the younger Bragg, aged only twenty-five, was in France developing sound-ranging techniques to help the allies in the war against Germany to fix the coordinates of enemy artillery batteries. He remains the youngest person ever to win a Nobel. Years later Max Perutz summed up the range of discoveries that subsequently flowed from the Braggs’ achievement:
Why water boils at 100°[C] and methane at -161°, why blood is red and grass is green, why diamond is hard and wax is soft, why graphite writes on paper and silk is strong, why glaciers flow and iron gets hard when you hammer it, how muscles contract, how sunlight makes plants grow and how living organisms have been able to evolve into ever more complex forms … The answers to all these problems have come from structural analysis.3
Knighted in 1920, Sir William Bragg moved to London as Professor of Physics at University College (UCL), and then Director of the Davy-Faraday Laboratory at the Royal Institution (RI), a post that he held from 1923 until his death in 1942. A central figure in British science, he was also President of the Royal Society from 1935 until 1940. Long before ‘public understanding of science’ became a topic of debate, Bragg retained the nineteenth-century assumption that new discoveries in science should be part of public discourse, and was an enthusiastic writer and speaker. In 1919 he gave the Christmas Lectures for children at the Royal Institution on the subject ‘Concerning the Nature of Things’; six years later he again fascinated his young audience with his series ‘Old Trades and New Knowledge’. Both series were published as books, and contained some of the first public descriptions of the capacity of X-ray crystallography to open up new perspectives:
The discovery of X-rays has increased the keenness of our vision … a thousand times, and we can now ‘see’ the individual atoms and molecules.4
From the early 1920s Bragg began to use X-ray crystallography to investigate organic molecules (those containing carbon, which include all the molecules that make up living things) rather than the simple, inorganic salts that his son continued to work on as a very young professor at Manchester. Now well into his sixties and with heavy administrative responsibilities at the RI, Sir William recruited young men and women to join his endeavour in the laboratories where Humphry Davy and Michael Faraday had conducted their chemical and electrical experiments a century before.
Bill Astbury (FRS 1940), the son of a potter from Stoke on Trent, had gone to Cambridge on a scholarship and graduated with a First in Natural Sciences. Joining Bragg as a postgraduate at UCL and the RI, he began to use X-ray diffraction to study the structure of natural fibres such as wool that are made of large, complex protein molecules. In 1928 he moved to the University of Leeds, an important centre of the textile industry, where he continued to develop the technique of fibre diffraction. During the 1930s he was the first to take X-ray photographs of DNA fibres (long before anyone had established its significance as the molecule of heredity). Although he was not able to obtain definitive structures, his insights into the ‘coiled’ nature of these molecules were fundamental to later discoveries by Linus Pauling (the alpha helix of proteins) and Maurice Wilkins, Rosalind Franklin, James Watson and Francis Crick (the DNA double helix).
Kathleen Yardley (later Lonsdale, FRS 1945) was the tenth child of an Irish postmaster who had a drink problem. Her mother brought the family to England for a better life, and in 1922 Yardley graduated from Bedford College (a women’s college of London University) with the highest mark in physics that anyone in the university had achieved for ten years. Bragg immediately wrote to recruit her as his research assistant. When she married fellow researcher Thomas Lonsdale and had three children, Bragg kept her supplied with work she could do at home, then found her a grant to pay for domestic help so that she could come back to the lab. This concern to create conditions in which a married woman could pursue a scientific career was wholly exceptional at the time, as was Thomas Lonsdale’s willingness to share domestic chores and support his wife in her career. Kathleen Lonsdale clarified the structure of a number of small organic molecules, notably confirming that benzene was a flat ring of six carbon atoms, each with a hydrogen attached.
Tiny, courageous and independent, Lonsdale dealt with glass ceilings by refusing to see them, and achieved a series of notable firsts for British women in science. In 1945 she and Marjorie Stephenson, the Cambridge biochemist, signed the Register of Fellows of the Royal Society, the first women to do so since its foundation in 1660. Their election followed delicate political manoeuvring largely on the part of the then President, Sir Henry Dale (who became Lonsdale’s boss at the RI after William Bragg’s death in 1942) to overturn what prejudice remained among the Fellowship after legal obstacles were removed in 1919. She also benefited from the energetic advocacy of her erstwhile fellow graduate student, Bill Astbury. It was his presentation of a correctly drawn up certificate of her candidacy that prompted Dale to win the majority of the Fellowship over to this revolutionary move.5
In 1949 Lonsdale became the first woman to be appointed to a professorship at University College London, and in 1968 the first to become President of the British Association for the Advancement of Science. A Quaker and conscientious objector, in 1943 she refused to pay the fine of £2 for nonregistration for civil defence work, an action that earned her a month in Holloway prison. Appalled at the monotony of prison life, she became an active supporter of prison reform after her release. At the height of the Cold War she wrote a book, Is Peace Possible?,6 giving a personal response to her ‘sense of corporate guilt and responsibility that scientific knowledge should have been so misused’ as to develop atomic weapons. Her example was an inspiration to the generations of women crystallographers who followed.
Also born in Ireland, to a comfortably-off farming family, John Desmond Bernal7 had astonished his Cambridge tutors as an undergraduate by producing unbidden an eighty-page manuscript giving mathematical derivations of the 230 ‘space groups’ of classical crystallography. The diversion of his efforts probably cost him a First, but left them in no doubt of his quick grasp of theoretical concepts, and like Astbury he came to Bragg with their enthusiastic recommendation. Though he never completed a PhD thesis, during his time at the RI he solved the structures of single crystals, notably graphite, designed the X-ray goniometer that all crystallographers used to mount and photograph their crystals for years afterwards, and made further theoretical contributions to the subject. In 1927 he returned to Cambridge as the first Lecturer in Structural Crystallography in the department of mineralogy.
THE SAGE OF SCIENCE
Bernal was a polymath, able to discourse convincingly and at length on any topic from Chinese art to quantum physics. While still an undergraduate he had earned the nickname ‘Sage’ from his fellow students: the name stuck throughout his life, used by all his friends and colleagues with barely a trace of irony. Nor were his energies confined to intellectual pursuits. Exchanging devout Roman Catholicism for equally devout Marxism as an undergraduate, he became a leading member of the ‘visible college’ of scientists and socialists who came to prominence in the 1930s.8 Always linking thought to action, he was an indefatigable organiser, notably of the Association of Scientific Workers and later its international counterpart, the World Federation of Scientific Workers. His desire for experimentation extended far outside the laboratory: he pursued a private life of unabashed promiscuity, justified to himself and others by his political mission to escape the restrictions of social convention.
Bernal was unusual among scientists in the degree to which he reflected on his experiences and beliefs in both public and private. In his early life he kept diaries charting everything from his scientific and political insights to his sexual conquests, and at the age of only twenty-five began a passionate and idealistic memoir (never published) entitled Microcosm. Soon afterwards he produced his first published book, The World, the Flesh and the Devil: An Enquiry into the Future of the Three Enemies of the Rational Soul (1929), which accurately predicted a number of scientific developments including the Apollo space programme, and just as inaccurately forecast the triumph of world Communism. A later and much more influential book, The Social Function of Science (1939), argued for central planning of science on the Soviet model, with the goal of improving human welfare rather than pursuing knowledge for its own sake.
The Second World War gave Bernal the opportunity to put his own science to the service of society. He was involved in studies of the accuracy of bombing raids and their effects, which influenced both civil defence policy and Bomber Command, and conducted surveys of the Normandy coastline and seabed as part of the preparation for the D-day landings. After the war he aligned himself, like many of his fellow scientists, with opposition to nuclear warfare, coining the phrase ‘weapons of mass destruction’ at a speech to the British-Soviet Society in London in 1949. His influence might have been greater had it not been for his blindly uncritical support for Soviet Communism, which was unwavering in the face of Stalin’s purges, the Lysenko affair and the invasion of Hungary. His accusation that the direction of Western science was dictated by warmongers led to his removal from the Council of the British Association for the Advancement of Science. Despite his valuable service during the war years, he never received any honours in Britain.
The double Nobel Prize-winner Linus Pauling (For.Mem.RS 1949) is one of many who described Bernal as the most brilliant scientist they had ever met. Yet he never personally made the kind of breakthrough that would have set him on the road to Stockholm. With so much to do, and so little time, he rarely pursued a scientific project to its conclusion. Instead, he gathered around him a group of able disciples of both sexes and showered them with ideas. They did not let him down.
PROTEINS AND PRIZES
Dorothy Crowfoot (later Hodgkin9) was a slim, soft-spoken, first-class graduate in chemistry from Oxford who came to Bernal’s lab in 1932 to begin a PhD. The eldest of four girls, Crowfoot came from a middle-class family who did not see intellectual pursuits as off-limits for women. Her father was a colonial administrator and archaeologist, and her mother, without any formal higher education, became a world expert in ancient textiles. It was she who encouraged Crowfoot’s schoolgirl interest in chemistry by giving her W.H. Bragg’s collected lectures to read, and his account of crystallography captured her imagination.
Crowfoot excelled in all the practical aspects of crystallography - growing the crystals, mounting them and photographing them - but also had a remarkable ability to visualise the three-dimensional manipulations that the early, trial-and-error stage of the subject demanded. She quickly became Bernal’s right hand, conducting preliminary observations on the dozens of crystals that poured into his lab from all over the world. Asked later how she succeeded so early, she modestly replied that there was so much gold lying about, one could not help picking it up.10
One day Glenn Millikan, a young scientist and friend of Bernal’s, returned to Cambridge from Sweden with a tube of crystals of the digestive enzyme pepsin in his pocket. Like all enzymes pepsin is a protein, one of a class of biological molecules that are the precision tools of the living body. Enzymes are highly specific catalysts that speed the construction and destruction of all the body’s constituents; other proteins include keratin and collagen that build strong structures such as hair and skin, antibodies that protect us against disease, and hormones such as insulin. All proteins depend for their function on their molecular structure. With care they can be purified and crystallised just like simple salts (though the crystals tend to be very small). The fact that they crystallise at all implies that their molecules have a regular structure - something that not all chemists believed at the time - and Bernal was convinced that solving these structures would reveal the ‘secret of life’.
When he took the pepsin crystals out of the liquid in the tube he found that they quickly lost their crystalline form, so he mounted a crystal with some of the liquid inside a fine glass capillary before putting it in the X-ray beam. He obtained a pattern of spots, the first time anyone had successfully made a single protein crystal diffract. Crowfoot went on to take a further series of photographs of the crystal until they had enough for a letter to Nature,11 describing their preliminary observations. Protein molecules are so large, consisting of thousands of atoms arranged in folded chains, that the relationship between their X-ray reflections and atomic positions is far from straightforward. Trial-and-error methods could not begin to narrow down the range of possible structures that would produce such patterns. Nevertheless, the Bernal and Crowfoot paper heralded the modern era of protein structure analysis.
Already at the forefront of the field at the age of twenty-four, in 1934 Crowfoot returned to Oxford where Somerville College (a women-only college) had given her a fellowship, and embarked on an X-ray study of the protein hormone insulin.12 She married the historian Thomas Hodgkin, and despite his long absences promoting adult education in the north of England, had given birth to two children by the end of 1941. A supportive college, indulgent in-laws and cheap domestic labour enabled her to keep working with only the briefest of intervals, despite a severe attack of acute rheumatoid arthritis after the birth of her first child. During the Second World War she was recruited to the secret penicillin project, trying to solve the structure of the miraculously effective antibiotic that had been purified from mould by Howard Florey and his colleagues in Oxford’s Dunn School of Pathology. Penicillin molecules had only a couple of dozen atoms, but the substance proved difficult to crystallise.
Success followed in 1945 after Kathleen Lonsdale personally brought Hodgkin samples of a more easily crystallisable penicillin derivative from America, where efforts to start industrial production were under way. Hodgkin’s structure unequivocally confirmed the presence of a previously unseen ring of atoms in the molecule, known as a beta lactam ring, that was fundamental to the drug’s ability to incapacitate bacteria. Although this discovery did not immediately lead to the creation of synthetic antibiotics as the project’s industrial partners had hoped, it was one of the first examples of a drug’s function being explained in terms of its structure, a principle that underlies all drug discovery programmes today. Lonsdale was delighted, and hoped for the opportunity to exercise her brand-new status as a Royal Society Fellow on Hodgkin’s behalf:
I am going to ask a favour; when this work is published, may I communicate it [to the Proceedings of the Royal Society]? If … it is possible I think that it would be rather pleasant that a woman Fellow should communicate such a very important paper by another woman, and I would be very proud to do it.13
As she had so fervently wished, Hodgkin was herself elected to the Royal Society two years later, aged only thirty-six and by then a mother of three. She went on to solve the structure of the anti-pernicious anaemia factor, Vitamin B12, and in 1960 the Society appointed her its first Wolfson Research Professor. Bernal’s prophecy came true when she was awarded the 1964 Nobel Prize for Chemistry, the first (and so far the only) British woman to win a science Nobel. The following year she was appointed to the Order of Merit, the first woman to receive the honour since Florence Nightingale.
While Hodgkin developed Bernal’s project in Oxford, another of his students kept it going in Cambridge after Bernal himself had departed for the chair in physics at Birkbeck in 1937. Max Perutz (FRS 1954)14came to Cambridge as a wealthy foreign research student, funded by an allowance from his father who ran a textile business in Vienna. He began work on the protein haemoglobin, the pigment in red blood cells that carries oxygen round the body. But with the Anschluss in 1938 his Jewish family lost everything and had to flee for their lives. His parents eventually arrived in Cambridge and became dependent on his support. Fortunately his excellent X-ray photographs of haemoglobin crystals so impressed the new Cavendish Professor of Physics - none other than Bragg junior, soon to be Sir Lawrence to distinguish him from his father - that he found himself taken on in 1939 as Bragg’s research assistant with a grant from the Rockefeller Foundation.
As an ‘enemy alien’, Perutz suffered internment in 1940-41, but on his return was recruited (thanks to Bernal, and to a brief pre-war foray into glaciology) to one of the most audacious scientific projects of the war. Project Habbakuk,15 misspelled and misguided, aimed to build a huge fleet of aircraft carriers out of ice to enable planes to refuel as they crossed the Atlantic. Perutz carried out successful experiments on making ice stronger, but the project ran for months before its American partners calculated that construction of the vessels would be hopelessly costly and impractical, and cancelled it. For Perutz, however, its value was incalculable: through it he gained a British passport and the security he had lacked for so long.
More successful wartime scientific projects, such as penicillin, code-breaking and radar, led the government to increase budgets for peacetime research. Perutz’s work on haemoglobin, championed by Bragg, seemed sufficiently promising for the Medical Research Council to fund a unit on the Molecular Structure of Biological Systems (later called simply Molecular Biology) in the Cavendish Laboratory, under Perutz’s leadership. The crowded but exceptionally well-equipped unit’s mix of physics, chemistry, biology and mathematics proved a magnet for curious minds, especially physicists who had become disillusioned with their subject after Hiroshima.
Francis Crick (FRS 1959) was one of these, joining Perutz’s unit in 1949 and contributing a new mathematical rigour to his studies of proteins. The restless young American geneticist James Watson (For.Mem.RS 1981) arrived two years later. Informed by fibre diffraction photographs by Maurice Wilkins (FRS 1959) and Rosalind Franklin at King’s College London, the two of them discovered the double helix structure of DNA in 1953.16 The structure was the most important discovery of twentieth-century biology, providing a mechanism that could unite Charles Darwin’s theory of evolution and Gregor Mendel’s model of heredity. A ‘spiral staircase’ of two linked chains of complementary pairs of the four nucleotide bases adenine, thymine, guanine and cytosine, it immediately revealed how such a chemically simple molecule could account for life in all its abundant diversity. ‘It has not escaped our notice’, famously wrote the authors of their classic paper in Nature,17 ‘that the specific pairing we have postulated immediately suggests a possible copying mechanism for the genetic material.’ Each chain could make a new double helix, enabling cells and organisms to replicate themselves. Crick and Watson also realised that the infinite number of ‘words’ that could be written in the four-letter alphabet A, T, G and C provided a genetic code to direct the construction of protein chains, though it took the efforts of many scientists until the mid-1960s to crack the code. The discovery ushered in the modern era of biotechnology, in which scientists not only read but edit genetic information to produce animals, plants, medicines or industrial processes tailored to human demands.
Perutz himself and his colleague John Kendrew (FRS 1960) continued with the much more difficult problem of protein structure. In 1953 Perutz discovered that introducing mercury atoms into the haemoglobin molecule could remove ambiguities in the results obtained from such large, irregular molecules. Combining this technique with pioneering computer analysis, Kendrew solved the structure of myoglobin, an oxygen-carrying protein a quarter of the size of haemoglobin, in 1957. Two years later Perutz and his team finally succeeded with haemoglobin. For the first time it was possible to see how the protein chain encoded by a DNA sequence folded itself into a characteristic, compact shape, as specific to its purpose as the nuts, bolts, valves, pistons, sparkplugs and gearwheels of a motor car. Perutz continued to work on haemoglobin for the rest of his life, describing the mechanism by which the ‘breathing molecule’ seizes and releases oxygen, exploring the evolutionary relationships between haemoglobins of different species, and linking abnormal haemoglobin to disease. Today’s structural biologists use essentially the same technique, though with much better X-ray sources and computer analysis, to explore the whole toolbox of molecular machines that make up the living body. These include the enzyme DNA polymerase that builds new DNA chains on the template of a single DNA strand, and the bacterial flagellar motor, a protein complex that rotates the tiny flails that propel bacteria through their fluid worlds.
In 1962 Perutz and Kendrew shared the Nobel Prize for Chemistry, while Crick, Watson and Wilkins received the accolade for Physiology: an extraordinary sweep for one country, let alone a single laboratory. Sir Lawrence Bragg had been instrumental in forwarding all their claims: he heard of the awards while recovering in hospital from an operation for prostate cancer, leading his doctor to tell his wife that he was ‘over the worst, but now I think he may die of excitement’.18 He had left Cambridge in 1953 to take up his father’s old job as Director of the Royal Institution. Having failed in his first plan of moving Perutz and Kendrew to the RI with him, Bragg started his own protein structure group there. It included David Phillips (FRS 1967), a young post-doctoral researcher from Cardiff, who led a team that solved the next protein structure, the enzyme lysozyme,19 in 1965. With his student Louise Johnson (FRS 1990), he was the first to shed light on the molecular interactions that give enzymes their catalytic effect, without which the chemical reactions that power our lives would be impossible.
Bragg dedicated his last years to restoring the RI, which had gone through a fallow period, to the glory days of Faraday or indeed his own father. Apart from sorting out its finances and establishing a first-class programme of research, he devoted most of his own energies to promoting science literacy. With enormous enjoyment and a knack for the felicitous analogy, he launched a year-round programme of lectures for schools, accompanied by the most spectacular demonstrations his inventive mind could conjure. Not a man for political activism, he took every opportunity through lecturing and broadcasting to present his vision of science as a benign, humanising activity that transcended class, gender and national boundaries. The RI continues this work today.
The triumphant successes of Cambridge molecular biology had been carried out largely in a ‘temporary’ shed outside the Cavendish Laboratory, known as The Hut. In 1962 they moved to the purpose-built Medical Research Council Laboratory of Molecular Biology, which has continued to expand ever since. Max Perutz chose to be chairman of the lab, not director as was usual in MRC units. He pursued a policy of attracting good people, giving them a share in the resources of the lab, and letting them get on with their research with a minimum of interference while he got on with his. The model also included more or less compulsory tea and coffee breaks in the communal canteen, where even the starriest prima donna would sit down next to the most junior graduate student and discuss science.
It paid off. The tally of Nobel Prize-winners steadily rose, with Fred Sanger (his second), Cesar Milstein, Georges Köhler, Aaron Klug, John Walker, Sydney Brenner, Robert Horvitz, John Sulston and Venkatramen Ramakrishnan joining the list. In 1993 Sulston (FRS 1986) moved to become founding director of the nearby Wellcome Trust Sanger Institute. Its major role in the international Human Genome Project, which published the complete human sequence in 2003, grew directly from Sulston’s work at the LMB on sequencing the genome of the nematode worm, work supported by Jim Watson in his role as head of the US Office of Genome Research. Both the LMB and the Sanger Institute continue as international centres of molecular biology, while labs throughout the world are peopled with those who imbibed the LMB philosophy as young researchers. Sulston, supported by the Wellcome Trust, has continued to champion the free availability of biological information and oppose ‘land grabs’ in the genome for private gain.20
Perutz retired as chairman of the LMB in 1979, but never gave up research. In his latter years he became a frequent contributor to the New York Review of Books, writing witty and lucid essay-reviews on science and scientists. Though he abhorred political extremes of both right and left, he shared Bernal’s view of science as a force for good and set out to counter the anti-science movement with his 1989 collection of essays Is Science Necessary?21 His main concern was to promote health and well-being in developing countries, and to that end he advocated birth control, intensive agriculture and nuclear power (later with reservations). Like his more politically motivated colleagues, he argued passionately for an end to nuclear weapons and indeed all forms of warfare:
A nuclear war would destroy everything that has been built up over centuries without giving us any control over what, if anything, will rise from the ashes. We must work for the application of science to peace and a more just distribution of its benefits to mankind.
As for John Kendrew, after his solution of myoglobin he turned to government advice and scientific organisation. He had a close exposure to nuclear matters during two years’ tenure as deputy to the chief scientific adviser of the Ministry of Defence at the time of the Polaris Sales Agreement between Britain and the US. He subsequently became a member of the Council for Scientific Policy, created under the Labour government in 1964, and was knighted. A committed internationalist, he chaired the International Council of Scientific Unions and in 1978 became the founding director of the European Molecular Biology Laboratory, now a flourishing centre for research and training in the subject with a membership of twenty European countries.
On Sir Lawrence Bragg’s retirement from the RI, David Phillips moved his group to Oxford. His successors there, Louise Johnson and Dave Stuart (FRS 1996), have in turn headed the life sciences division at the Diamond Light Source, the synchrotron near Didcot in Oxfordshire that since 2007 has provided a national source of high-energy X-rays to probe ever more complex biological molecules and their interactions. Phillips himself spent his last two decades in scientific administration. As Chairman of the Advisory Board for the Research Councils from 1983-93, he shouldered the difficult and thankless task of sharing out an essentially static science budget among a growing and increasingly high-tech scientific community, while constantly fighting for better settlements from the government. After being raised to the peerage, he chaired the House of Lords Select Committee on Science and Technology.
Dorothy Hodgkin remained a practising scientist well into her eighties, by which time she was chronically disabled with arthritis. In 1969 her dedicated team of assistants and students finally completed the task she set herself in 1934, of revealing the structure of insulin. It was a result that depended on huge advances in technology, including the development of high-speed computers and innovative ways of programming them. No single individual could have done all this. Protein crystallography offers a prime example of a style of science that is the antithesis of the ‘lone genius’ model. It is often said to be a science in which women excel, though most are wary of any suggestion that it is ‘women’s work’. It is the case, however, that Hodgkin took on many female graduate students who went on to make careers in the field.
Hodgkin was another political idealist and admirer of Communist systems. Like Bernal she had found that her political sympathies made her persona non grata in the US during the McCarthy era (and like Bernal she was awarded the Lenin Peace Prize); but unlike him she conducted her politics on a personal level and avoided strident sloganising. She maintained contacts with colleagues in China throughout the Cultural Revolution, and worked indefatigably behind the scenes to bring about their readmission into international scientific organisations. She was a vocal opponent of war and nuclear weapons, a stance that led to her appointment in 1975 as President of the Pugwash Conferences on Science and World Affairs.22 She was not afraid to use her status as a Nobel Prize-winner in the service of causes she believed in. She personally lobbied education minister Sir Keith Joseph over cuts in the higher education budget, and Prime Minister Margaret Thatcher (who was her former student) on East-West relations; and she insisted on speaking out about the Israeli-Palestinian conflict at a conference of Nobel Prize-winners organised by the French President François Mitterrand in 1988. She is commemorated in the Dorothy Hodgkin Fellowships, launched by the Royal Society to help young scientists, especially women, to get on to the academic career ladder.
Bernal never gave up science, taking on the presidency of the International Union of Crystallography in 1963. In the post-war years science policy in both Europe and the US moved a considerable distance in the direction he had mapped out in his 1939 book. The establishment of ‘big science’ projects such as the Apollo programme, CERN,23 and the Human Genome Project all required central government planning and support. The Labour Prime Minister Harold Wilson’s ‘white heat [of the scientific revolution]’ speech in 1963, and the UK’s science policy White Papers A Framework for Government Research and Development (1971), Realising Our Potential (1993) and Excellence and Opportunity (2000), all stressed wealth creation and the quality of life, though the debate has swung back and forth over whether scientists themselves or their government paymasters should set the agenda. Once again, though, Bernal’s take on the interdependence of science and socialism has proved laughably wide of the mark. When he wrote, in 1964, that ‘the scientific and computer age is necessarily a socialist one’,24 he could not have envisaged the commercial free-for-all made possible by the World Wide Web.
Like all branches of science, X-ray analysis calls for a combination of imagination and rigorous data collection. Unlike some, it gives hard-earned results that no paradigm shift or new experimental approach can undermine. As Perutz wrote, ‘Bragg’s structures were not preliminary approximations subject to revision: any student setting out to redetermine the structures of calcite, quartz or beryl will be disappointed.’ 25The knowledge that an exact solution existed gave crystallographers an optimism that kept them going in their darkest hours (insulin took thirty-five years to solve, haemoglobin twenty-two). It is perhaps no coincidence that the scientists in this account were prepared to tackle society’s problems in the same hopeful spirit.
1 Hilary Rose, Love, Power and Knowledge: Towards a Feminist Transformation of the Sciences (Cambridge, Polity, 1994), p. 117.
2 For more on the Braggs, see Graeme Hunter, Light is a Messenger: The Life and Science of William Lawrence Bragg (Oxford, Oxford University Press, 2004).
3 Letter from Max Perutz to Gerald Holton, 9 July 1966, private papers, quoted in Georgina Ferry, Max Perutz and the Secret of Life (London, Chatto & Windus, 2007), p. 28.
4 W.H. Bragg, Concerning the Nature of Things (London, G. Bell & Sons, 1925).
5 Rose, Love, Power and Knowledge, pp. 115-35.
6 Kathleen Lonsdale, Is Peace Possible? (London, Penguin, 1957).
7 For more on Bernal, see Andrew Brown, J.D. Bernal: The Sage of Science (Oxford, OUP, 2005).
8 See Gary Werskey, The Visible College: A Collective Biography of British Scientists and Socialists of the 1930s (London, Allen Lane, 1978).
9 For more on Hodgkin, see Georgina Ferry, Dorothy Hodgkin: A Life (London, Granta, 1998).
10 Lewis Wolpert and Alison Richards, A Passion for Science (Oxford, OUP, 1988).
11 J.D. Bernal and D. Crowfoot, ‘X-ray Photographs of Crystalline Pepsin’, Nature, 133 (1934), 794-5.
12 Insulin controls levels of glucose in the bloodstream, and has to be given artificially to those with some forms of diabetes.
13 Kathleen Lonsdale to Dorothy, 15 May 1945, Bodleian Library, Hodgkin papers, H.138. In fact the work was published not in the Royal Society journal but as part of a book edited by Hans Clarke and others, The Chemistry of Penicillin, published by Princeton University Press in 1949.
14 For more on Perutz, see Ferry, Max Perutz and the Secret of Life.
15 It was conceived by Geoffrey Pyke, a maverick inventor whom Bernal regarded as a genius and persuaded Louis Mountbatten, Chief of Combined Operations, to take seriously.
16 J.D. Watson, The Double Helix (London, Weidenfeld & Nicolson, 1968); Robert Olby, The Path to the Double Helix (London, Macmillan, 1974).
17 J.D. Watson and F.H.C Crick, ‘A structure for deoxyribose nucleic acid’, Nature, 171 (1953), 737-8.
18 Quoted in Hunter (2004), pp. 232.
19 Found in tears and other secretions, lysozyme provides some protection against bacterial infection.
20 John Sulston and Georgina Ferry, The Common Thread: A Story of Science, Politics, Ethics and the Human Genome (London, Bantam, 2002).
21 Max Perutz, Is Science Necessary? (London, Barrie & Jenkins, 1989).
22 Pugwash is an international organisation of scientists and others dedicated to research into the dangers of nuclear weapons. It was inspired by the Russell-Einstein Manifesto of 1955.
23 The European Centre for Nuclear Research in Geneva.
24 J.D. Bernal, ‘After Twenty-Five Years’ in M. Goldsmith and A. McKay (eds), The Science of Science (London, Souvenir Press, 1964).
25 Max Perutz, ‘How W.L. Bragg Invented X-ray Analysis’ in Max Perutz, I Wish I’d Made You Angry Earlier (expanded edition) (New York, Cold Spring Harbor Laboratory Press, 2003).