Chapter 26.1 How the structure of lysozyme was actually determined
Crystallography of biological macromolecules
First Online Edition (2006)
Part 26. A historical perspective
Published Online: 1 JAN 2006
© International Union of Crystallography 2006
International Tables for Crystallography
How to Cite
Blake, C. C. F., Fenn, R. H., Johnson, L. N., Koenig, D. F., Mair, G. A., North, A. C. T., Oldham, J. W. H., Phillips, D. C., Poljak, R. J., Sarma, V. R. and Vernon, C. A. 2006. How the structure of lysozyme was actually determined. International Tables for Crystallography. F:26:26.1:745–772.
- Published Online: 1 JAN 2006
Lysozyme was the second protein structure and the first enzyme structure to be solved by X-ray diffraction methods. The structure was published in 1965. Later work published in 1967 led to an explanation of the catalytic function of the enzyme and gave a vision of the explanatory power of structure for biological function. This chapter describes the crystals, the search for heavy-atom derivatives and the careful X-ray measurements made possible by the development of the linear diffractometer. By optimizing crystal mounting, by correcting for absorption effects and with considerable attention to radiation-damage effects implemented in the measurements and in the data-processing software, a complete data set to 2 Å resolution was measured with remarkable precision. The precision of the measurements allowed anomalous-scattering effects to be introduced to help resolve the phase problem. The resulting electron-density map was immediately interpretable and the initial draft model building took about 1 month. The model was completed in time for it to form the centrepiece of Sir Lawrence Bragg’s 75th birthday party at the Royal Institution on 31 March 1965. Many of the historical details of the data collection and structure determination are presented for the first time.
- absorption corrections;
- data processing;
- early structure determinations;
- heavy-atom derivatives;