Author： Leonard Gordon McCarthy Joanne Nurizzo Didier Thibault Xavier
Publisher： Taylor & Francis Ltd
ISSN： 0894-0886
Source： Synchrotron Radiation News, Vol.20, Iss.3, 2007-05, pp. : 18-24
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Abstract
During the last twenty years macromolecular crystallography (MX) has become the predominant tool for the investigation of structure/function relationships in biology. This is due to many technological advances and, in particular, improved access to synchrotron radiation (SR) sources, data from which has lead to ∼80% of the macromolecular crystal structures currently being deposited in the Protein Data Bank (PDB) (Figure 1, http://www.rcsb.org). The demand for synchrotron beam-time is also being fuelled by the funding of a number of structural genomics programmes [1], which, following an initial investment in protein production technology, have now contributed ∼1000 new structures to the PDB.
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