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

G. Joliff (1) , P. Beguin (1) , J. Millet (1) , Jp Aubert (1) , Pedro Maria Alzari (1) , M. Juy (1) , Rj Poljak (1)

1 IBCP - Institut de biologie et chimie des protéines [Lyon]

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.

Domaines: Biochimie, Biologie Moléculaire

G. Joliff, P. Beguin, J. Millet, Jp Aubert, Pedro Maria Alzari, et al.. Crystallization and preliminary X-ray diffraction study of an endoglucanase from Clostridium thermocellum.. Journal of Molecular Biology, 1986, 189, pp.249-250. ⟨hal-00313144⟩