Open AccessCrystallization and preliminary X‐ray diffraction of the Munc18c–syntaxin4 1–29 complex
Author(s) -
Latham Catherine F.,
Hu ShuHong,
Gee Christine L.,
Armishaw Chris J.,
Alewood Paul F.,
James David E.,
Martin Jennifer L.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107022361
Subject(s) - crystallization , crystallography , diffraction , resolution (logic) , materials science , x ray crystallography , protein crystallization , drop (telecommunication) , diffusion , chemistry , optics , physics , organic chemistry , thermodynamics , telecommunications , artificial intelligence , computer science
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 P 2 1 3, with unit‐cell parameters a = b = c = 170.8 Å, α = β = γ = 90°, were generated that diffract to 3.7 Å resolution on a laboratory X‐ray source.