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Crystallization and preliminary X-ray crystallographic analysis of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5

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JournalActa Crystallographica Section D: Biological Crystallography
DatePublished - May 1999
Volume55
Number of pages3
Pages (from-to)1058-1060
Original languageEnglish

Abstract

Crystals of the catalytic core domain of a Trichoderma reesei beta-mannanase belonging to glycoside hydrolase family 5 have been grown by the sitting-drop method at room temperature using ammonium sulfate as precipitant. The crystals grow as thin colourless plates and belong to space group P2(1), with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 Angstrom, beta = 111.3 degrees, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 Angstrom resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 Angstrom at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.

    Research areas

  • SEQUENCE-BASED CLASSIFICATION, SACCHAROMYCES-CEREVISIAE, CRYSTAL-STRUCTURE, ENDOGLUCANASE, CELLULASE, COMPLEX, DOMAIN, GENE

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