- PII
- S3034551025060207-1
- DOI
- 10.7868/S3034551025060207
- Publication type
- Article
- Status
- Published
- Authors
- Volume/ Edition
- Volume 70 / Issue number 6
- Pages
- 1042-1047
- Abstract
- Molecular dynamics simulations revealed a notable thermal stability of the precursor cluster of proteinase K crystals (a dimer formed prior to crystallization) within the 20–60°C temperature range. This finding led to the hypothesis that crystallization at an atypically elevated temperature (50–60°C) could be feasible. This theoretical prediction was subsequently confirmed experimentally: proteinase K crystals were successfully grown after incubation at 60°C. The results not only demonstrate the predictive power of the molecular dynamics approach employed here for identifying optimal protein crystallization conditions, but also open new opportunities for capturing the catalytically relevant conformation of proteinase K.
- Keywords
- Date of publication
- 12.09.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 7
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