5g26 | pdb_00005g26

Unveiling the Mechanism Behind the in-meso Crystallization of Membrane Proteins

spinqualitylabelsall models 5g26, resolution 2.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g26 is a 1 chain structure with sequence from Escherichia coli o157. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 97M, 97N Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The structural changes occurring at the nanoscale level within the lipid bilayer and driving the in-meso formation of large well-diffracting membrane protein crystals have been uniquely characterized for a model membrane protein, intimin. Importantly, the order to order transitions taking place within the bilayer and the lipidic nanostructures required for crystal growth have been shown to be general, occurring for both the cubic and the sponge mesophase crystallization pathways. For the first time, a transient fluid lamellar phase has been observed and unambiguously assigned for both crystallization pathways, present at the earliest stages of protein crystallogenesis but no longer observed once the crystals surpass the size of the average lyotropic liquid crystalline domain. The reported time-resolved structural investigation provides a significantly improved and general understanding of the nanostructural changes taking place within the mesophase during in-meso crystallization which is a fundamental advance in the enabling area of membrane protein structural biology. The nanoscience behind the art of in-meso crystallization of membrane proteins.,Zabara A, Meikle TG, Newman J, Peat TS, Conn CE, Drummond CJ Nanoscale. 2017 Jan 5;9(2):754-763. doi: 10.1039/c6nr07634c. PMID:27976759 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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