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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Feb 1;62(Pt 2):113-6. Epub 2006 Jan 27.

Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian MSS4-Rab8 GTPase protein complex.

Author information

1
Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.

Abstract

Rab GTPases function as ubiquitous key regulators of membrane-vesicle transport in eukaryotic cells. MSS4 is an evolutionarily conserved protein that binds to exocytotic Rabs and facilitates nucleotide release. The MSS4 protein in complex with nucleotide-free Rab8 GTPase has been purified and crystallized in a form suitable for structure analysis. The crystals belonged to space group P1, with unit-cell parameters a = 40.92, b = 49.85, c = 83.48 A, alpha = 102.88, beta = 97.46, gamma = 90.12 degrees. A complete data set has been collected to 2 A resolution.

PMID:
16511278
PMCID:
PMC2150963
DOI:
10.1107/S1744309105042995
[Indexed for MEDLINE]
Free PMC Article

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