期刊
NATURE METHODS
卷 9, 期 12, 页码 1212-U119出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.2248
关键词
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资金
- contract research 'Forschungsprogramm Methoden fur die Lebenswissenschaften' of the Baden-Wurttemberg Stiftung
- European Union [261863]
- Deutsche Forschungsgemeinschaft [HA 5918/1-1, SFB 766, SFB 740]
- Leibniz Society
- Max Planck Society
Membrane proteins are largely underrepresented among available atomic-resolution structures. The use of detergents in protein purification procedures hinders the formation of well-ordered crystals for X-ray crystallography and leads to slower molecular tumbling, impeding the application of solution-state NMR. Solid-state magic-angle spinning NMR spectroscopy is an emerging method for membrane-protein structural biology that can overcome these technical problems. Here we present the solid-state NMR structure of the transmembrane domain of the Yersinia enterocolitica adhesin A (YadA). The sample was derived from crystallization trials that yielded only poorly diffracting microcrystals. We solved the structure using a single, uniformly C-13- and N-15-labeled sample. In addition, solid-state NMR allowed us to acquire information on the flexibility and mobility of parts of the structure, which, in combination with evolutionary conservation information, presents new insights into the autotransport mechanism of YadA.
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