Crystallization of the catalytic domain of Clostridium cellulolyticum CeIF cellulase in the presence of a newly synthesized cellulase inhibitor
- 1 January 1998
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 54 (1) , 114-118
- https://doi.org/10.1107/s090744499700797x
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-β-cellobiosyl-4-thio-β-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 Å. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 Å.Keywords
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