Expression, purification, crystallization and preliminary X‐ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis

Expression, purification, crystallization and preliminary X‐ray crystallographic studies of a... The Antarctic psychrophile Pseudoalteromonas haloplanktis produces a cold‐active cellulase. To date, a three‐dimensional structure of a psychrophilic cellulase has been lacking. Crystallographic studies of this cold‐adapted enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of the cold adaptation and the high catalytic efficiency of the enzyme at low and moderate temperatures. The catalytic core domain of the psychrophilic cellulase CelG from P. haloplanktis has been expressed, purified and crystallized and a complete diffraction data set to 1.8 Å has been collected. The space group was found to be P212121, with unit‐cell parameters a = 135.1, b = 78.4, c = 44.1 Å. A molecular‐replacement solution, using the structure of the mesophilic counterpart Cel5A from Erwinia chrysanthemi as a search model, has been found. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section D Wiley

Expression, purification, crystallization and preliminary X‐ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis

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Publisher
Wiley
Copyright
Copyright © 2003 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1399-0047
eISSN
1399-0047
DOI
10.1107/S0907444903008849
Publisher site
See Article on Publisher Site

Abstract

The Antarctic psychrophile Pseudoalteromonas haloplanktis produces a cold‐active cellulase. To date, a three‐dimensional structure of a psychrophilic cellulase has been lacking. Crystallographic studies of this cold‐adapted enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of the cold adaptation and the high catalytic efficiency of the enzyme at low and moderate temperatures. The catalytic core domain of the psychrophilic cellulase CelG from P. haloplanktis has been expressed, purified and crystallized and a complete diffraction data set to 1.8 Å has been collected. The space group was found to be P212121, with unit‐cell parameters a = 135.1, b = 78.4, c = 44.1 Å. A molecular‐replacement solution, using the structure of the mesophilic counterpart Cel5A from Erwinia chrysanthemi as a search model, has been found.

Journal

Acta Crystallographica Section DWiley

Published: Jul 1, 2003

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