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Crystallization and preliminary X-ray diffraction study of an endoglucanase from Clostridium thermocellum

Authors :
Joliff, G.
Beguin, P.
Millet, J.
Aubert, Jp
Alzari, Pedro Maria
Juy, M.
Poljak, Rj
Deleage, Gilbert
Publication Year :
1986
Publisher :
HAL CCSD, 1986.

Abstract

Endoglucanase D, a cellulose degradation enzyme from Clostridium thermocellum has been cloned in Escherichia coli, purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12) with a = 57.7 (+/- 0.1) A, c = 192.1 (+/- 0.2) A, and diffract X-rays to a resolution of 2.8 A. They are suitable for a high-resolution X-ray diffraction analysis.Endoglucanase D, a cellulose degradation enzyme from Clostridium thermocellum has been cloned in Escherichia coli, purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12) with a = 57.7 (+/- 0.1) A, c = 192.1 (+/- 0.2) A, and diffract X-rays to a resolution of 2.8 A. They are suitable for a high-resolution X-ray diffraction analysis.

Details

Language :
English
Database :
OpenAIRE
Accession number :
edsair.od.......166..204ee43c14f17b3ea88e20054a6f5484