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

E Sabini, A M Brzozowski, M Dauter, G J Davies, K S Wilson, M Paloheimo, P Suominen, M Siika-Aho, M Penttila

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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.

Original languageEnglish
Pages (from-to)1058-1060
Number of pages3
JournalActa Crystallographica. Section D, Biological Crystallography
Volume55
Publication statusPublished - May 1999

Keywords

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

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