Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian MSS4-Rab8 GTPase protein complex.
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.
Itzen
Aymelt
A
Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Bleimling
Nathalie
N
Ignatev
Alexander
A
Pylypenko
Olena
O
Rak
Alexey
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000302:isolation & purification*; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D051379:Mice; D020691:rab GTP-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*
D020662:Guanine Nucleotide Exchange Factors; C489794:RABIF protein, human; D020558:GTP Phosphohydrolases; D020691:rab GTP-Binding Proteins