by Susan Gillmor
The widespread impression of Rosalind Franklin stems from James Watson’s unflattering description of her in his Double Helix retelling of the discovery of structure of DNA [1]. He took an uncharitable pot-shot at his deceased colleague, though she made major contributions in three different fields and her contribution to the DNA structure solution came at a high price. Her death from ovarian cancer probably came as a result of X-ray exposure during the alignment of the instrument, on which she captured the famed DNA helical structure, without proper shielding. The one-dimensional view of her presented in Watson’s book is both incorrect and, unfortunately, its sexism was typical of the time. In reality, her life reflects a complex woman and a formidable scientist [2-4].
The oldest girl of five children in an upper middle-class family, Franklin excelled in school and developed scholarly habits well before entering into Newnham College, Cambridge University. During her studies and later her career, she maintained a weekly correspondence with her family. The letters outlined her exam anxieties, lab successes and other details of her life. Atypical of the time, she exhibited a zest for rugged camping, gallivanting around Europe, the US, and her home British Isles as scientific conferences and family holidays permitted.
Her graduation from Newnham in 1941 led her into the war effort at the University of Cambridge. Her dissertation investigated the porosity of coal, a practical consideration during times of shortage, and led to her PhD in 1945. She used classic physical chemistry techniques to determine the adsorption of gases and liquids into various grades of coal. Her experiments contributed to a clutch of papers examining coal pore size and classifying it as a function of its fuel performance based on porosity characteristics [5-7]. At the close of WWII, she took advantage of a connection with Adrienne Weill, a French Chemist and friend, to land a position in Laboratoire Central des Services Chimiques de l'Etat in Paris. She became a member of Jacques Mering’s Lab and there, typical of a post-doctoral position, she learned a new skill, X-ray crystallography. As a natural progression in her coal research, she used X-rays on amorphous carbon [7-11]. By all accounts, Franklin’s time in Paris was happy and memorable. She pursued science in an atmosphere of equality with a cosmopolitan backdrop of Paris recovering from the war.
She returned to England as a research associate connected to John Randall’s lab in King’s College, to study biological structures using X-ray crystallography. In contrast to Paris, her new environment was marked by a more provincial outlook and an ‘old boy’s club’ atmosphere. She set up a X-ray system to look at biological samples. Crucially, she devised a chamber with humidity control to allow her to investigate two different forms of DNA, both the A (dry) and the B (wet). Franklin was given the impression that she would be working on DNA herself, but Maurice Wilkins was working on it simultaneously. The two were equals, and Franklin treated the relationship as such, however to most of her colleagues, she was regarded as his subordinate.
As a successful scientist, she did not suffer fools. Her critique of Francis Crick and Watson’s initial DNA structure, with the phosphate groups paired inward, was not kind. The electrostatic repulsion was an obvious impediment. However, Linus Pauling made a similar mistake in his ill-fated triple helix structure [12]. Crick and Watson were in good company. By the time Wilkins allowed Crick and Watson to view Franklin’s critical X-ray film, the working relationship between Wilkins and Franklin was toxic. His sharing of her DNA X-ray data without her knowledge or consent was a major breach of protocol and trust. Crick and Watson’s insight into the base pairing and the helical arrangement remains a monumental achievement. From Franklin’s notebooks, she was on the right track but had not made the leap to solve the B form of the DNA structure. The Nature publications in April of 1953 of Crick and Watson on the DNA double helix model; Wilkins, Alex Stokes and Herbert Wilson on DNA X-ray data, and Franklin and Raymond Gosling on the arrangements of the phosphate backbone and bases are phenomenal feats reflective of the scientific talents of all involved [13-15].
From the DNA Nature publications to her death in 1958, Franklin continued her scientific contributions. She set up her own research lab at Birkbeck College and focused on the Tobacco Mosaic Virus, solving its structure in a series of papers [16-23]. She was honored for his accomplishment within her own lifetime and participated in making a model of it for the exhibit at the Brussels’ World Fair in 1958.
Her role in solving the DNA structure was not the total sum of her short career and was not even the most recognized achievement in her lifetime. The Nobel Prize to Crick, Watson and Wilkins in 1962 occurred after her death. Their lack of recognition to her role in the Nobel speeches did not go unnoticed. Only Wilkins even mentioned her X-ray contributions [24-26]. Now Franklin is more famous for that slight than her science, which is unfortunate. Had her career not been cut short by her death at age 37, her continued contributions would have cemented her role as distinguished scientist in X-ray crystallography and biophysics.
REFERENCES
[1] J.D. Watson, A. Gann, J. Witkowski, The Annotated and Illustrated Double Helix Annotated ed., Simon & Schuster, New York, 2012.
[2] J. Glynn, My Sister Rosalind Franklin, Oxford University Press, Oxford, 2012.
[3] B. Maddox, Rosalind Franklin: The Dark Lady of DNA, Haper Collins Publishers, Hmmersmith, London, 2002.
[4] A. Sayre, Rosalind Franklin and DNA, W. W. Norton and Company, Inc, New York, 1975.
[5] D.H. Bangham, F. R., Thermal Expansion of Coals and Carbonised Coals., Transactions of the Faraday Society 48 (1946) 289-295.
[6] R. Franklin, A Study of the Fine Structure of Carbonaceous Solids by Measurements of True and Apparent Densities: Part I. Coals, Transactions of the Faraday Society, 45 (1949) 274-286.
[7] R. Franklin, On the Structure of Carbon, The Journal de Chimie Physique et de Physico-Chimie Biologique, 47 (1950) 573-575.
[8] R.E. Franklin, Influence of the bonding electrons on the scattering of X-rays by carbon, Nature, 165 (1950) 71-71.
[9] R.E. Franklin, The interpretation of diffuse X-ray diagrams of carbon, Acta Crystallographica, 3 (1950) 107-121.
[10] R.E. Franklin, A rapid approximate method for correcting low-angle scattering measurements for the influence of the finite height of the X-ray beam, Acta Crystallographica, 3 (1950) 158-159.
[11] R.E. Franklin, The structure of graphitic carbons, Acta Crystallographica, 4 (1951) 253-261.
[12] L. Pauling, R.B. Corey, A Proposed Structure For The Nucleic Acids, Proceedings of the National Academy of Sciences of the United States of America, 39 (1953) 84-97.
[13] R.E. Franklin, R.G. Gosling, Molecular configuration in sodium thymonucleate, Nature, 171 (1953) 740-741.
[14] J.D. Watson, F.H. Crick, Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid, Nature, 171 (1953).
[15] M.H.F. Wilkins, A.R. Stokes, H.R. Wilson, Molecular structure of deoxypentose nucleic acids, Nature, 171 (1953).
[16] R.E. Franklin, Structure of tobacco mosaic virus, Nature, 175 (1955) 379-381.
[17] R.E. Franklin, X-ray diffraction studies of cucumber virus 4 and three strains of tobacco mosaic virus, Biochim Et Biophys Acta, 19 (1956) 203-211.
[18] R.E. Franklin, D.L.D. Caspar, A. Klug, The structure of viruses as determined by X-ray diffraction, 1959.
[19] R.E. Franklin, B. Commoner, Abnormal protein associated with tobacco mosaic virus. X-rav diffraction by an abnormal protein (B8) associated with tobacco mosaic virus, Nature, 175 (1955) 1076-1077.
[20] R.M. Franklin, H. Rubin, C. Davis, The preparation, purification and properties of Newcastle disease virus labeled with radiophosphorus, Virology, 3 (1957) 96-114.
[21] A. Klug, R.E. Franklin, The reaggregation of the A-protein of tobacco mosaic virus, Biochimica et biophysica acta, 23 (1957) 199-201.
[22] R.E. Franklin, K.C. Holmes, The helical arrangement of the protein sub-units in tobacco mosaic virus, Biochim Et Biophys Acta, 21 (1956) 405-406.
[23] R.E. Franklin, A. Klug, The nature of the helical groove on the tobacco mosaic virus particle. X-ray diffraction studies, Biochim Et Biophys Acta, 19 (1956) 403-416.
[24] <http://www.nobelprize.org/nobel_prizes/medicine/laureates/1962/ crick-lecture.html>
[25] <http://www.nobelprize.org/nobel_prizes/medicine/laureates/1962/ watson-lecture.html>
[26] <http://www.nobelprize.org/nobel_prizes/medicine/laureates/1962/ wilkins-lecture.html>