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.
|Authors||Latham, C. F.;Hu, S. H.;Gee, C. L.;Armishaw, C. J.;Alewood, P. F.;James, D. E.;Martin, J. L. :|
|Publisher Name||ACTA CRYSTALLOGR F|
|Published Issue||Pt 6|
|URL link to publisher's version||http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17554178|
|OpenAccess link to author's accepted manuscript version||https://publications.gimr.garvan.org.au/open-access/2231|