Crystallization and preliminary X-ray diffraction of the Munc18c-syntaxin4 (1-29) complex.
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.
Latham
Catherine F
CF
Institute for Molecular Bioscience and Special Research Centre for Functional and Applied Genomics, The University of Queensland, Brisbane, QLD, Australia.
Hu
Shu Hong
SH
Gee
Christine L
CL
Armishaw
Chris J
CJ
Alewood
Paul F
PF
James
David E
DE
Martin
Jennifer L
JL
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
D046912:Multiprotein Complexes; D051938:Munc18 Proteins; D010446:Peptide Fragments; D050765:Qa-SNARE Proteins