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Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile pseudomonas aeruginosa

✍ Scribed by Vincent Villeret; Jozef Van Beeumen; Jean-Pierre Chessa; Charles Gerday

Book ID
105356492
Publisher
Cold Spring Harbor Laboratory Press
Year
2008
Tongue
English
Weight
342 KB
Volume
6
Category
Article
ISSN
0961-8368

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✦ Synopsis

A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P2(1)2(1)2(1). A complete data set to 2.1 A resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R-factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an alpha-amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme.

πŸ“œ SIMILAR VOLUMES

Crystallization and preliminary X-ray di
Crystallization and preliminary X-ray diffraction studies of Ξ±-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
✍ Nushin Aghajari; Richard Haser; Georges Feller; Charles Gerday πŸ“‚ Article πŸ“… 1996 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 208 KB

## Abstract A cold‐active α‐amylase was purified from culture supernatants of the antarctic psychrophile __Alteromonas haloplanctis__ A23 grown at 4 Β°C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold‐adapted enzyme have