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, (...

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Published inActa crystallographica. Section F, Structural biology and crystallization communications Vol. 63; no. Pt 6; pp. 524 - 528
Main Authors Latham, Catherine F, Hu, Shu Hong, Gee, Christine L, Armishaw, Chris J, Alewood, Paul F, James, David E, Martin, Jennifer L
Format Journal Article
LanguageEnglish
Published England 01.06.2007
Subjects
Animals
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DEHYDRATION
DIFFUSION
INTERFACES
MEMBRANES
Mice
Multiprotein Complexes - chemistry
Munc18 Proteins - chemistry
Peptide Fragments - chemistry
Qa-SNARE Proteins - chemistry
RESOLUTION
SCREENING
SPACE GROUPS
X-RAY DIFFRACTION
X-RAY SOURCES
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Summary: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.
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ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309107022361