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

Bostjan Kobe, Johann Deisenhofer

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Ribonuclease inhibitor was purified from pig liver and crystallized at 21°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 Å and c = 83.6 Å, and diffract to better than 3 Å resolution. Self rotation functions and packing density of the crystals are consistent with two molecules in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)137-140
Number of pages4
JournalJournal of Molecular Biology
Volume231
Issue number1
DOIs
StatePublished - May 1993

Keywords

  • Crystallization
  • Leucine-rich repeats
  • Preliminary X-ray data
  • Ribonuclease inhibitor

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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