CRYSTALLIZATION OF PORCINE LIVER RIBONUCLEASE INHIBITOR A MEMBER OF THE FAMILY OF PROTEINS CONTAINING LEUCINE-RICH REPEATS

Ulf Neumann, Jan Hofsteenge, Anita H. Arkema, Bauke W. Dijkstra

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Abstract

Single crystals of the RNase inhibitor from porcine liver have been obtained from 30 to 34 % saturated ammonium sulphate solutions at pH 6.0 to 7.2, containing 20 mM dithiothreitol, at room temperature over a period of two to three weeks. Because the inhibitor contains 30 1/2-cystinyl residues, all of which occur in the free thiol form, crystallization experiments were carried out in a desiccator under a nitrogen atmosphere. The crystals belong to the tetragonal space group I4, with cell dimensions a = b = 134.76 Å and c = 83,65 Å. The asymmetric part of the unit cell contains two molecules with a molecular mass of 49,093 Da, as could be shown with a self-rotation function calculated in the resolution range 10.0 to 3.2 Å. The crystals diffract to at least 3.2 Å resolution and are suitable for an X-ray structure determination.
Original languageEnglish
Pages (from-to)505-508
Number of pages4
JournalJournal of Molecular Biology
Volume231
Issue number2
DOIs
Publication statusPublished - 20-May-1993

Keywords

  • CRYSTALLIZATION
  • RIBONUCLEASE INHIBITOR
  • LEUCINE-RICH REPEAT
  • X-RAY DIFFRACTION
  • HUMAN-PLACENTA
  • SACCHAROMYCES-CEREVISIAE
  • KINETIC CHARACTERIZATION
  • ADENYLYL CYCLASE
  • DROSOPHILA
  • ANGIOGENIN
  • YEAST
  • GENE
  • PURIFICATION
  • SUPERFAMILY

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