Crystallization and preliminary crystallographic studies of giα1 and mutants of giα1 in the GTP and GDP-bound states

David E. Coleman, Ethan Lee, Mark B. Mixon, Maurine E. Linder, Albert M. Berghuis, Alfred G. Gilman, Stephen R. Sprang

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

Several different crystal forms of Giα1 have been grown and analyzed. Crystals of native protein containing bound GTPγS belong to space group P3121 or P3221 with cell dimensions a, b = 80·6 Åand c = 106·3 Å and diffract to a resolution of 1·9 Å using synchrotron radiation. Crystals of native protein containing bound GDP belong to space group I4 with cell dimensions a, b = 121·3 Å, and c = 67·7 Å and diffract to 3·0Å. Data sets from crystals grown using mutant proteins have also been obtained and characterized.

Original languageEnglish (US)
Pages (from-to)630-634
Number of pages5
JournalJournal of Molecular Biology
Volume238
Issue number4
DOIs
StatePublished - May 12 1994

Keywords

  • G proteins
  • GTP binding proteins
  • Protein crystallization
  • Signal transduction
  • X-ray diffraction

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Structural Biology

Fingerprint

Dive into the research topics of 'Crystallization and preliminary crystallographic studies of giα1 and mutants of giα1 in the GTP and GDP-bound states'. Together they form a unique fingerprint.

Cite this