Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum.
J Mol Biol
; 235(4): 1348-50, 1994 Jan 28.
Article
en En
| MEDLINE
| ID: mdl-8308898
The catalytic domain of a thermostable xylanase from Clostridium thermocellum has been expressed in Escherichia coli and crystallized from a polyethylene glycol 2000 solution by the hanging drop method. Crystals belong to the triclinic space group P1 with cell dimensions a = 46.8 A, b = 50.8 A, c = 70.3 A, alpha = 100.7 degrees, beta = 83.8 degrees, gamma = 101.6 degrees, and two molecules in the unit cell. These crystals diffract X-rays to at least 1.8 A resolution and are suitable for high-resolution X-ray analysis.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Clostridium
/
Glicósido Hidrolasas
Idioma:
En
Revista:
J Mol Biol
Año:
1994
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Países Bajos