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

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 A. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 A.