Crystallization and preliminary X-ray analysis of the Clostridium thermocellum cellulosome xylanase Z feruloyl esterase domain

Citation
Dl. Blum et al., Crystallization and preliminary X-ray analysis of the Clostridium thermocellum cellulosome xylanase Z feruloyl esterase domain, ACT CRYST D, 56, 2000, pp. 1027-1029
Citations number
21
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
8
Pages
1027 - 1029
Database
ISI
SICI code
0907-4449(200008)56:<1027:CAPXAO>2.0.ZU;2-0
Abstract
Feruloyl esterases cleave ferulic acid from arabinoxylan and pectin. Ferulo yl groups are believed to crosslink the polysaccharide chain within the pol ymer and to link hemicellulose to lignin, which may play a role in controll ing the growth of plants. The Clostridium thermocellum cellulosome xylanase Z feruloyl esterase was expressed in Escherichia coli, purified and crysta llized. The crystals diffract to 2.4 Angstrom resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 43.14 , b = 63.77, c = 79.57 Angstrom. Assuming one molecule per asymmetric unit, the Matthews coefficient is calculated to be 1.87 Angstrom(3) Da(-1), whic h corresponds to a solvent content of 34%.