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Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin
Open accessAbstract
The charge density distribution of a protein has been refined experimentally. Diffraction data for a crambin crystal were measured to ultra-high resolution (0.54 Å) at low temperature by using short-wavelength synchrotron radiation. The crystal structure was refined with a model for charged, nonspherical, multipolar atoms to accurately describe the molecular electron density distribution. The refined parameters agree within 25% with our transferable electron density library derived from accurate single crystal diffraction analyses of several amino acids and small peptides. The resulting electron density maps of redistributed valence electrons (deformation maps) compare quantitatively well with a high-level quantum mechanical calculation performed on a monopeptide. This study provides validation for experimentally derived parameters and a window into charge density analysis of biological macromolecules.
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Cited by
Best, R. B., Zhu, X., Shim, J., Lopes, P. E. M., Mittal, J., Feig, M., & MacKerell, A. D. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300400x · Cited by 4,532
Putnam, C. D., Hammel, M., Hura, G. L., & Tainer, J. A. (2007) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583507004635 · Cited by 1,184
The performance of semilocal and hybrid density functionals in 3d transition-metal chemistry
Furche, F., & Perdew, J. P. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2162161 · Cited by 572
Antimicrobial Peptides from Plants
Tam, J., Wang, S., Wong, K., & Tan, W. (2015) · Pharmaceuticals · doi:10.3390/ph8040711 · Cited by 489
Fragment molecular orbital method: use of approximate electrostatic potential
Nakano, T., Kaminuma, T., Sato, T., Fukuzawa, K., Akiyama, Y., Uebayasi, M., & Kitaura, K. (2002) · Chemical Physics Letters · doi:10.1016/s0009-2614(01)01416-6 · Cited by 428
Metadata
- Authors
- Jelsch, C., Teeter, M. M., Lamzin, V., Pichon-Pesme, V., Blessing, R. H., & Lecomte, C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-03-28
- Volume
- 97
- Issue
- 7
- Pages
- 3171-3176
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2143534385
- Cited by
- 223
- References
- 0
- FWCI
- 9.34
- Type
- journal article
- Language
- en
- Open access
- green
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- Jelsch, C., Teeter, M. M., Lamzin, V., Pichon-Pesme, V., Blessing, R. H., & Lecomte, C. (2000). Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.97.7.3171
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