Sixty years from discovery to solution: crystal structure of bovine liver catalase form III

Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):756-62. doi: 10.1107/S0907444911024486. Epub 2011 Aug 9.

Abstract

The crystallization and structural characterization of bovine liver catalase (BLC) has been intensively studied for decades. Forms I and II of BLC have previously been fully characterized using single-crystal X-ray diffraction. Form III has previously been analyzed by electron microscopy, but owing to the thinness of this crystal form an X-ray crystal structure had not been determined. Here, the crystal structure of form III of BLC is presented in space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 173.7, c = 186.3 Å. The asymmetric unit is composed of the biological tetramer, which is packed in a tetrahedron motif with three other BLC tetramers. This higher resolution structure has allowed an assessment of the previously published electron-microscopy studies.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Catalase / chemistry*
  • Catalase / ultrastructure
  • Cattle
  • Liver / enzymology*
  • Microscopy, Electron
  • X-Ray Diffraction

Substances

  • Catalase