title: Crystallization and preliminary X-ray diffraction of the Munc18c-syntaxin4 (1-29) complex.
abstract: The production of diffraction-quality crystals of Munc18c, a protein involved in regulating vesicular exocytosis in mammals, is reported. The diffraction resolution of Munc18c crystals was optimized by (i) cocrystallizing with a peptide fragment of the Munc18c functional binding partner syntaxin4, (ii) using nanolitre free-interface diffusion crystallization-screening chips and microlitre hanging-drop vapour diffusion and (iii) applying a post-crystallization dehydration treatment. Crystals belonging to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 170.8 A, alpha = beta = gamma = 90 degrees , were generated that diffract to 3.7 A resolution on a laboratory X-ray source.
authors.affiliation: Institute for Molecular Bioscience and Special Research Centre for Functional and Applied Genomics, The University of Queensland, Brisbane, QLD, Australia.
authors.forename: Catherine F
authors.initials: CF
authors.lastname: Latham
authors.forename: Shu Hong
authors.initials: SH
authors.lastname: Hu
authors.forename: Christine L
authors.initials: CL
authors.lastname: Gee
authors.forename: Chris J
authors.initials: CJ
authors.lastname: Armishaw
authors.forename: Paul F
authors.initials: PF
authors.lastname: Alewood
authors.forename: David E
authors.initials: DE
authors.lastname: James
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Martin
mesh_terms: D000818:Animals; D003460:Crystallization; D051379:Mice; D046912:Multiprotein Complexes / Q000737:chemistry*; D051938:Munc18 Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D050765:Qa-SNARE Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D046912:Multiprotein Complexes; D051938:Munc18 Proteins; D010446:Peptide Fragments; D050765:Qa-SNARE Proteins