Crystallization and preliminary X-ray studies of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011

J Mol Biol. 1994 Mar 18;237(1):163-4. doi: 10.1006/jmbi.1994.1216.

Abstract

Large crystals of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. 1011, a typical alkalophilic enzyme, have been obtained at room temperature using polyethylene glycol 3000 and 2-propanol as precipitant. They belong to the triclinic space group P1 with the following unit cell constants: a = 64.93 A, b = 74.45 A, c = 79.12 A, alpha = 85.2 degrees, beta = 105.0 degrees and gamma = 101.0 degrees. The crystallographic asymmetric unit seems to contain two molecules of CGTase, with crystal volume per protein mass (Vm) of 2.41 A3/Da and solvent content of 49% by volume. The crystals diffract to at least 2.0 A resolution and they are suitable for X-ray analysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Glucosyltransferases / chemistry*

Substances

  • Glucosyltransferases
  • cyclomaltodextrin glucanotransferase