4ycr

Structure determination of an integral membrane protein at room temperature from crystals in situ

spinqualitylabelsall models 4ycr, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ycr is a 1 chain structure with sequence from Haemophilus influenzae Rd KW20. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: BOG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TEHA_HAEIN Ion channel involved in potassium tellurite resistance. Publication Abstract from PubMed The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 A resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines. Structure determination of an integral membrane protein at room temperature from crystals in situ.,Axford D, Foadi J, Hu NJ, Choudhury HG, Iwata S, Beis K, Evans G, Alguel Y Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1228-37. doi:, 10.1107/S139900471500423X. Epub 2015 May 14. PMID:26057664 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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