Accurate protein crystallography at ultra-high resolution: Valence electron distribution in crambin

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, nonsphe...

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Pubblicato in:	Proc Natl Acad Sci U S A
Autori principali:	Jelsch, Christian, Teeter, Martha M., Lamzin, Victor, Pichon-Pesme, Virginie, Blessing, Robert H., Lecomte, Claude
Natura:	Artigo
Lingua:	Inglês
Pubblicazione:	National Academy of Sciences 2000
Soggetti:	Biological Sciences
Accesso online:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC16211/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10737790/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.97.7.3171
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