David W. Green (biochemist)

Last updated
David W. Green
Died1976
EducationUniversity of Cambridge (Ph.D.)
OccupationCrystallographer
EmployerUniversity of Edinburgh

David W. Green ( - 1976) was a crystallographer at the Medical Research Council Unit for the Study of the Molecular Structure of Biological Systems, Cavendish Laboratory, University of Cambridge.

David W. Green was a graduate student in the laboratory of Max Perutz at the University of Cambridge from 1952 to 1955 and obtained a Ph.D. [1] [2] He is known for demonstrating the first use of isomorphous replacement to solve the phase problem in X-ray crystallography. [3]

After completing his Ph.D., Green moved to the Davy-Faraday Research Laboratory at The Royal Institution in autumn 1955. [4]

He was recruited by Linus Pauling [5] but ultimately moved to MIT to work with Alexander Rich. [6] With Rich, Green solved the structure of N-methyluracil. [7] After his postdoctoral work, he returned to the Davy-Faraday Research Laboratory at The Royal Institution in London, England to continue his crystallographic research. [8] Later he moved to the Department of Physics at the University of Edinburgh. [9] In Edinburgh, Green was a senior lecturer and ran a group in solid state physics. [10]

Green died in 1976. [10]

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References

  1. Biology, ©2020 MRC Laboratory of Molecular; Avenue, Francis Crick; Campus, Cambridge Biomedical; CB2 0QH, Cambridge; Uk. 01223 267000. "LMB Alumni List". MRC Laboratory of Molecular Biology. Retrieved 2020-03-21.
  2. Perutz, Max (1997). Science is Not a Quiet Life. World Scientific Publishing Co. p. 66. doi:10.1142/3204. ISBN   978-981-02-2774-6.
  3. Green, D. W.; Ingram, V. M.; Perutz, M. F. (1954-09-14). "The structure of haemoglobin - IV. Sign determination by the isomorphous replacement method". Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences. 225 (1162): 287–307. Bibcode:1954RSPSA.225..287G. doi:10.1098/rspa.1954.0203. ISSN   0080-4630. S2CID   96889917.
  4. Aragó López, Carmen; Gonzalo, Julio A. (2003). Great solid state physicists of the 20th century . World Scientific. pp.  106. ISBN   981-238-336-0. OCLC   248978057.
  5. "March 22, 1958 - Linus Pauling Day-by-Day - Special Collections". scarc.library.oregonstate.edu. Retrieved 2020-03-21.
  6. Rich, Alexander (2004-06-01). "The Excitement of Discovery". Annual Review of Biochemistry. 73 (1): 1–37. doi: 10.1146/annurev.biochem.73.011303.073945 . ISSN   0066-4154. PMID   15189135.
  7. Green, D. W.; Mathews, F. S.; Rich, A. (November 1962). "The crystal and molecular structure of N-methyluracil". The Journal of Biological Chemistry. 237 (11): 3573–3575. doi: 10.1016/S0021-9258(19)70860-6 . ISSN   0021-9258. PMID   13950062.
  8. Aschaffenburg, R.; Green, D. W.; Simmons, R. M. (1965-08-01). "Crystal forms of β-lactoglobulin". Journal of Molecular Biology. 13 (1): 194–201. doi:10.1016/S0022-2836(65)80089-4. ISSN   0022-2836. PMID   5859035.
  9. Sawyer, L.; Green, D. W. (1979-07-25). "The reaction of cow β-lactoglobulin with tetracyanoaurate(III)". Biochimica et Biophysica Acta (BBA) - Protein Structure. 579 (1): 234–239. doi:10.1016/0005-2795(79)90102-8. ISSN   0005-2795. PMID   37917.
  10. 1 2 Woolfson, Michael (2005). "William Cochran. 30 July 1922 – 28 August 2003: Elected FRS 1962". Biographical Memoirs of Fellows of the Royal Society. 51: 67–85. doi: 10.1098/rsbm.2005.0005 . ISSN   0080-4606.