Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina
- Biosciences Division, Argonne National Laboratory, Argonne, IL 60439 (United States)
- Fermentation Biotechnology Research Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, Illinois 61604 (United States)
- Institute of Chemistry, Slovak Academy of Sciences, 845 38 Bratislava (Slovakia)
The catalytic domain of the glucuronoyl esterase from H. jecorina was overexpresssed, purified and crystallized in space group P2{sub 1}2{sub 1}2{sub 1}. X-ray diffraction data were collected to 1.9 Å resolution. 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{sub 1}2{sub 1}2{sub 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.
- OSTI ID:
- 22360521
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 4; Other Information: PMCID: PMC2374253; PMID: 18391420; PUBLISHER-ID: ll5145; OAI: oai:pubmedcentral.nih.gov:2374253; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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