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

Abstract

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… (More)

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@article{ReverbelLeroy1998CrystallizationOT, title={Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor.}, author={C Reverbel-Leroy and Goetz Parsiegla and Vincent Moreau and Michel Juy and C{\'e}cile Tardif and Hugues Driguez and Jean Pierre Belaich and Resul Haser}, journal={Acta crystallographica. Section D, Biological crystallography}, year={1998}, volume={54 Pt 1}, pages={114-8} }