Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data

The physical properties that determine the propensity of a protein to form a well-ordered crystal suitable for structure determination are poorly understood. An analysis of large-scale crystallization results generated by a structural genomics consortium highlights the importance of low-entropy surf...

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Veröffentlicht in:	Nature biotechnology 2009-01, Vol.27 (1), p.51-57
Hauptverfasser:	Price II, W Nicholson, Chen, Yang, Handelman, Samuel K, Neely, Helen, Manor, Philip, Karlin, Richard, Nair, Rajesh, Liu, Jinfeng, Baran, Michael, Everett, John, Tong, Saichiu N, Forouhar, Farhad, Swaminathan, Swarup S, Acton, Thomas, Xiao, Rong, Luft, Joseph R, Lauricella, Angela, DeTitta, George T, Rost, Burkhard, Montelione, Gaetano T, Hunt, John F
Format:	Artikel
Sprache:	eng
Schlagworte:	Agriculture Algorithms Amino acids analysis Animals BASIC BIOLOGICAL SCIENCES Bioinformatics Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biomedicine Biophysics - methods Biotechnology Computational Biology - methods CONTROL CORRELATIONS CRYSTALLIZATION DATA Data mining DIFFRACTION METHODS Entropy Epitopes - chemistry EXPERIMENTAL DATA GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE Genomics HUMAN POPULATIONS Humans INTERACTIONS Life Sciences MINING Models, Statistical national synchrotron light source PHYSICAL PROPERTIES Physiological aspects PROBABILITY Properties Protein Folding PROTEIN STRUCTURE PROTEINS Proteins - chemistry STABILITY Structure SUPPORTS Surface Properties SURFACES THERMODYNAMICS
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