Crystallization and preliminary X-ray investigation of a ubiquitin carrier protein (E2) from Arabidopsis thaliana

  • William J. Cook
  • , Leigh C. Jeffrey
  • , Michael L. Sullivan
  • , Richard D. Vierstra

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Crystals of a recombinant ubiquitin carrier protein from Arabidopsis thaliana have been grown from solutions of ammonium sulfate. The crystals are orthorhombic, space group P212121; the axes are a = 41.8(1) A ̊, b = 44.9(1) A ̊ and c = 83.2(1) A ̊. The crystals are quite stable to X-rays and diffract beyond 2.1 Åresolution. There is one molecule in the asymmetric unit.

Original languageEnglish
Pages (from-to)1183-1186
Number of pages4
JournalJournal of Molecular Biology
Volume223
Issue number4
DOIs
StatePublished - Feb 20 1992

Keywords

  • crystallization
  • protein crystallofraphy
  • ubiquitin
  • ubiquitin carrier protein

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