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Direct Observation of Protein Solvation and Discrete Disorder with Experimental Crystallographic Phases
Abstract
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.
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Cited by
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417
Biological Water: Femtosecond Dynamics of Macromolecular Hydration
Pal, S. K., Peon, J., Bagchi, B., & Zewail, A. H. (2002) · The Journal of Physical Chemistry B · doi:10.1021/jp0213506 · Cited by 494
[28] Phase determination from multiwavelength anomalous diffraction measurements
Hendrickson, W. A., & Ogata, C. M. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76074-9 · Cited by 349
Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains
Lundell, A., Olin, A. I., Mörgelin, M., al-Karadaghi, S., Aspberg, A., & Logan, D. T. (2004) · Structure · doi:10.1016/j.str.2004.05.021 · Cited by 127
Metadata
- Authors
- Burling, F. T., Weis, W. I., Flaherty, K. M., & Brünger, A. T.
- Venue
- Science
- Published
- 1996-01-05
- Volume
- 271
- Issue
- 5245
- Pages
- 72-77
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2024534366
- Cited by
- 241
- References
- 0
- FWCI
- 25.33
- Type
- journal article
- Language
- en
- Open access
- closed
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- Burling, F. T., Weis, W. I., Flaherty, K. M., & Brünger, A. T. (1996). Direct Observation of Protein Solvation and Discrete Disorder with Experimental Crystallographic Phases. Science. https://doi.org/10.1126/science.271.5245.72
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
