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Macromolecular Crystallographic Computing
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Author(s): Kostas Bethanis (Agricultural University of Athens, Greece), Petros Giastas (Hellenic Pasteur Institute, Greece), Trias Thireou (Agricultural University of Athens, Greece)and Vassilis Atlamazoglou (Agricultural University of Athens, Greece)
Copyright: 2010
Pages: 36
Source title:
Biocomputation and Biomedical Informatics: Case Studies and Applications
Source Author(s)/Editor(s): Athina A. Lazakidou (University of Peloponnese, Greece)
DOI: 10.4018/978-1-60566-768-3.ch001
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Abstract
Structural genomics or structural proteomics can be defined as the quest to obtain the three-dimensional structures of all proteins. Single-crystal X-ray crystallography provides the most direct, accurate and in most of the cases the only way of forming images of macromolecules. Using crystallography, threedimensional images have been made of thousands of macromolecules, especially proteins and nucleic acids. These give detailed information about their activity, their mechanism for recognizing and binding substrates and effectors, and the conformational changes which they may undergo. This chapter presents the basic crystallographic procedure steps and a thorough survey of the computational software used most frequently by protein X-ray crystallographers. The determination of the structure of 2[4Fe-4S] ferredoxin from Escherichia coli. is examined as a case study of implementation of these steps and programs. Finally, some of the perspectives of the field of computational X-ray crystallography are noted showing the future developments in the ceaseless evolution of new methods and proliferation of new programs.
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