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

Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1058-60. doi: 10.1107/s0907444999002140.

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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalysis
  • Crystallization
  • Crystallography, X-Ray
  • Fungal Proteins / chemistry*
  • Fungal Proteins / classification
  • Fungal Proteins / isolation & purification
  • Mannosidases / chemistry*
  • Mannosidases / classification
  • Mannosidases / isolation & purification
  • Trichoderma / enzymology*
  • beta-Mannosidase

Substances

  • Fungal Proteins
  • Mannosidases
  • beta-Mannosidase