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Slow cooling of protein crystals
Cryoprotectant-free thaumatin crystals have been cooled from 300 to 100 K at a rate of 0.1 K s(−1) – 10(3)–10(4) times slower than in conventional flash cooling – while continuously collecting X-ray diffraction data, so as to follow the evolution of protein lattice and solvent properties during cool...
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| Hoofdauteurs: | , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
International Union of Crystallography
2009
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2746722/ https://ncbi.nlm.nih.gov/pubmed/19798409 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0021889809023553 |
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