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Crystallization and preliminary X‐ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina
Author(s) -
Wood S. J.,
Li X.L.,
Cotta M. A.,
Biely P.,
Duke N. E. C.,
Schiffer M.,
Pokkuluri P. R.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108004594
Subject(s) - hypocrea , trichoderma reesei , esterase , materials science , crystallography , chemistry , enzyme , biochemistry , cellulase
The catalytic domain of the glucuronoyl esterase from Hypocrea jecorina (anamorph Trichoderma reesei ) was overexpresssed, purified and crystallized by the sitting‐drop vapor‐diffusion method using 1.4  M sodium/potassium phosphate pH 6.9. The crystals belonged to space group P 2 1 2 1 2 1 and X‐ray diffraction data were collected to 1.9 Å resolution. This is the first enzyme with glucoronoyl esterase activity to be crystallized; its structure will be valuable in lignocellulose‐degradation research.

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