Journal of Structural Biology, Vol.170, No.2, 184-191, 2010
50 years of fiber diffraction
In 1955 Ken Holmes started working on tobacco mosaic virus (TMV) as a research student with Rosalind Franklin at Birkbeck College, London. Afterward he spent 18 months as a post doc with Don Caspar and Carolyn Cohen at the Children's Hospital, Boston where he continued the work on TMV and also showed that the core of the thick filament of byssus retractor muscle from mussels is made of two-stranded alpha-helical coiled-coils. Returning to England he joined Aaron Klug's group at the newly founded Laboratory of Molecular Biology in Cambridge. Besides continuing the TMV studies, which were aimed at calculating the three-dimensional density map of the virus, he collaborated with Pringle's group in Oxford to show that two conformation of the myosin cross-bridge could be identified in insect flight muscle. In 1968 he opened the biophysics department at the Max Planck Institute for Medical Research in Heidelberg, Germany. With Gerd Rosenbaum he initiated the use of synchrotron radiation as a source for X-ray diffraction. In his lab the TMV structure was pushed to 4 A resolution and showed how the RNA binds to the protein. With his co-workers he solved the structure of g-actin as a crystalline complex and then solved the structure of the f-actin filament by orientating the g-actin structure so as to give the f-actin fiber diffraction pattern. He was also able to solve the structure of the complex of actin with tropomyosin from fiber diffraction. (C) 2010 Elsevier Inc. All rights reserved.
Keywords:Tobacco mosaic virus;Coiled-coils;Myosin cross-bridge;Actin;Tropomyosin;Synchrotron radiation