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Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina.

ABSTRACT: 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 P2(1)2(1)2(1) and X-ray diffraction data were collected to 1.9 A resolution. This is the first enzyme with glucoronoyl esterase activity to be crystallized; its structure will be valuable in lignocellulose-degradation research.

SUBMITTER: Wood SJ

PROVIDER: S-EPMC2374253 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina.

Wood S J SJ Li X-L XL Cotta M A MA Biely P P Duke N E C NE Schiffer M M Pokkuluri P R PR

Acta crystallographica. Section F, Structural biology and crystallization communications 20080321 Pt 4

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 P2(1)2(1)2(1) and X-ray diffraction data were collected to 1.9 A resolution. This is the first enzyme with glucoronoyl esterase activity to be crystallized; its structure will be valuable in lignocellulose-degradation researc ...[more]

PMID: 18391420

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