Abstract
Protein crystallography since the 1950’s has developed into one of the major arms of biology owing to its capacity to reveal the 3 dimensional structure in atomic detail of proteins and other macro-molecules. Because of this it has become an essential platform for understanding many biological processes. The success of protein X-ray analysis rests principally on the power of the experimental methods for determining the phase. In this technique heavy atoms which scatter X-rays strongly are introduced into the crystal — usually by soaking. Providing the crystal organisation is unaffected by this reaction the changes in the X-ray diffraction pattern can be used to locate the heavy atoms, then to calculate the phase angle and hence obtain the electron density from which the structure is interpreted.
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© 1987 Springer-Verlag Berlin Heidelberg
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Dodson, G. (1987). The Impact of Synchrotron Radiation on Protein Crystallography. In: Bianconi, A., Congiu Castellano, A. (eds) Biophysics and Synchrotron Radiation. Springer Series in Biophysics, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71490-0_1
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DOI: https://doi.org/10.1007/978-3-642-71490-0_1
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