Crystallization and preliminary X-ray crystallographic analysis of human Geminin coiled-coil domain.
Initially discovered in Xenopus laevis, Geminin is a DNA replication initiation inhibitor found in higher eukaryotes. The coiled-coil domain of Human Geminin (termed GemH-37) has been crystallized by the vapor-diffusion sitting-drop method. A complete 1.74 A data set has been collected on a single orthorhombic crystal with unit cell parameters a = 25.25, b = 44.35, c = 68.58 A. Successful molecular replacement shows that GemH-37 is a dimeric parallel coiled-coil. Structural analysis is now in progress.
Thépaut
Michael
M
Centre de Biochimie Structurale, CNRS UMR 5048 INSERM UMR 554, Faculté de Pharmacie, 15 Av Charles Flahault, 34060 Montpellier, France.
Hoh
François
F
Dumas
Christian
C
Calas
Bernard
B
Strub
Marie-Paule
MP
Padilla
André
A
D018797:Cell Cycle Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D064248:Geminin; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction / Q000379:methods; D029867:Xenopus Proteins
D018797:Cell Cycle Proteins; C577998:GMNN protein, Xenopus; C577995:GMNN protein, human; D064248:Geminin; D029867:Xenopus Proteins