Direct Observation of Protein Solvation and Discrete Disorder with Experimental Crystallographic Phases
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- F. Temple Burling
- F. T. Burling and A. T. Brünger, Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
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- William I. Weis
- W. I. Weis and K. M. Flaherty, Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
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- Kevin M. Flaherty
- W. I. Weis and K. M. Flaherty, Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
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- Axel T. Brünger
- F. T. Burling and A. T. Brünger, Howard Hughes Medical Institute and Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
書誌事項
- 公開日
- 1996-01-05
- DOI
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- 10.1126/science.271.5245.72
- 公開者
- American Association for the Advancement of Science (AAAS)
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説明
<jats:p>A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength anomalous dispersion (MAD) phasing. An accurate image of the crystal structure could thus be obtained without resort to phases calculated from a model. Partially reduced disulfide bonds, local disorder, and differences in the mobility of chemically equivalent molecules are apparent in the experimental electron density map. A solvation layer is visible that includes well-ordered sites of hydration around polar and charged protein atoms, as well as diffuse, partially disordered solvent shells around exposed hydrophobic groups. Because the experimental phases and the resulting electron density map are free from the influence of a model, they provide a stringent test of theoretical models of macromolecular solvation, motion, and conformational heterogeneity.</jats:p>
収録刊行物
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- Science
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Science 271 (5245), 72-77, 1996-01-05
American Association for the Advancement of Science (AAAS)