Crystallization and preliminary X-ray diffraction of the Munc18c-syntaxin4 (1-29) complex
| Autor: | Chris Armishaw, Christine L. Gee, David E. James, Shu Hong Hu, Catherine F. Latham, Jennifer L. Martin, Paul F. Alewood |
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| Rok vydání: | 2007 |
| Předmět: |
Diffraction
Peptide fragment Diffusion Biophysics Biochemistry law.invention Mice Munc18 Proteins X-Ray Diffraction Structural Biology law Genetics Animals Crystallization Chemistry Qa-SNARE Proteins Resolution (electron density) A protein Condensed Matter Physics Peptide Fragments Crystallography Crystallization Communications Multiprotein Complexes biological sciences X-ray crystallography Protein crystallization |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 6) |
| ISSN: | 1744-3091 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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