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

Elisabetta Sabini, Andrzej M. Brzozowski, Miroslawa Dauter, Gideon J. Davies, Keith S. Wilson, Marja Paloheimo, Pirkko Suominen, Matti Siika-Aho, Merja Penttilä

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

Crystals of the catalytic core domain of a Trichoderma reesei β-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 P21, with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 Å, β = 111.3°, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 Å resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 Å at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.

Original languageEnglish
Pages (from-to)1058-1060
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number5
DOIs
Publication statusPublished - 1 May 1999
MoE publication typeA1 Journal article-refereed

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