IMIS | Flanders Marine Institute
 

Flanders Marine Institute

Platform for marine research

IMIS

Publications | Institutes | Persons | Datasets | Projects | Maps
[ report an error in this record ]basket (0): add | show Printer-friendly version

Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis
Violot, S.; Haser, R.; Sonan, G.; Georlette, D.; Feller, G.; Aghajari, N. (2003). Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktis. Acta Crystallographica Section D-Structural Biology 59: 1256-1258. dx.doi.org/10.1107/S0907444903008849
In: Acta Crystallographica Section D-Structural Biology: Chester. ISSN 2059-7983, more
Peer reviewed article  

Available in  Authors 

Keyword
    Marine
Author keywords
    cellulase; extremophiles; psychrophilic enzymes

Authors  Top 
  • Violot, S.
  • Haser, R.
  • Sonan, G.
  • Georlette, D.
  • Feller, G., more
  • Aghajari, N.

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.

All data in IMIS is subject to the VLIZ privacy policy Top | Authors