Crystallization and preliminary X-ray analysis of porcine ribonuclease inhibitor, a protein with leucine-rich repeats

J Mol Biol. 1993 May 5;231(1):137-40. doi: 10.1006/jmbi.1993.1263.

Abstract

Ribonuclease inhibitor was purified from pig liver and crystallized at 21 degrees C from solutions containing dithiothreitol as an additive and ammonium sulfate, lithium sulfate or combinations of both as precipitants. Crystals have the symmetry of the tetragonal space group I4 with a = 134.9 A and c = 83.6 A, and diffract to better than 3 A resolution. Self rotation functions and packing density of the crystals are consistent with two molecules in the asymmetric unit.

MeSH terms

  • Animals
  • Crystallization
  • Intracellular Signaling Peptides and Proteins
  • Leucine*
  • Liver / metabolism
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / isolation & purification
  • Ribonucleases / antagonists & inhibitors
  • Swine
  • X-Ray Diffraction

Substances

  • Intracellular Signaling Peptides and Proteins
  • Proteins
  • ribonuclease inhibitor, porcine
  • Ribonucleases
  • Leucine