Complex between bovine ribonuclease A and porcine ribonuclease inhibitor crystallizes in a similar unit cell as free ribonuclease inhibitor

Bostjan Kobe, Zhiquan Ma, Johann Deisenhofer

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

We obtained three different morphologies of co-crystals of bovine ribonuclease A and porcine ribonuclease inhibitor. X-ray quality crystals were grown in 1.3 M ammonium sulfate, 100 mM sodium acetate (pH 5.0) and 20 mM dithiothreitol at 21 °C. These crystals have the symmetry of the tetragonal space group I4 with a=133.3 AÅ and c= 86.7 AÅ and diffract to 2.5 AÅ resolution; they have the same symmetry and only slightly different cell parameters than the crystals of free ribonuclease inhibitor. Polyacrylamide gel electrophoresis and the crystal density indicate that both ribonuclease inhibitor and ribonuclease A are present in the crystals. Although small, crystals are suitable for threedimensional structural analysis.

Original languageEnglish (US)
Pages (from-to)288-291
Number of pages4
JournalJournal of Molecular Biology
Volume241
Issue number2
DOIs
StatePublished - Aug 11 1994

Keywords

  • Complex
  • Crystallization
  • Leucine-rich repeats
  • Ribonuclease A
  • Ribonuclease inhibitor

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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