5avg

The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel

spinqualitylabelsall models 5avg, resolution 0.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5avg is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 0.95Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMed High-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries. Growth of protein crystals in hydrogels prevents osmotic shock.,Sugiyama S, Maruyama M, Sazaki G, Hirose M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Matsumura H J Am Chem Soc. 2012 Apr 4;134(13):5786-9. doi: 10.1021/ja301584y. Epub 2012 Mar, 27. PMID:22435400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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