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Effects of protein-crystal hydration and temperature on side-chain conformational heterogeneity in monoclinic lysozyme crystals
The modulation of main-chain and side-chain conformational heterogeneity and solvent structure in monoclinic lysozyme crystals by dehydration (related to water activity) and temperature is examined. Decreasing the relative humidity (from 99 to 11%) and decreasing the temperature both lead to contrac...
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| Pubblicato in: | Acta Crystallogr D Struct Biol |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
International Union of Crystallography
2018
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5892876/ https://ncbi.nlm.nih.gov/pubmed/29652254 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2059798318000207 |
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