Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor.

作者信息

Reverbel-Leroy C, Parsiegla G, Moreau V, Juy M, Tardif C, Driguez H, Bélaich J P, Haser R

机构信息

Université de Provence, Place Victor-Hugo, 13331 Marseille CEDEX 3, France.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):114-8. doi: 10.1107/s090744499700797x.

The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), by vapour diffusion, using PEG as a precipitant. The protein crystallizes in the orthorhombic P212121 space group and diffracts to a resolution of 2.0 A. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 A.