1ly0 | pdb_00001ly0

Structure of thaumatin crystallized in the presence of glycerol

spinqualitylabelsall models 1ly0, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ly0 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 1.36Å Ligands: TLA 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The intensely sweet protein thaumatin has been crystallized at 293 K in the presence of sodium tartrate and 25%(v/v) glycerol for X-ray diffraction data collection at 100 K. A comparison of the three-dimensional structure model derived from a crystal grown in the presence of glycerol with that of a control deprived of this additive reveals only minor changes in the overall structure but a approximately 20% reduction in the number of water molecules. X-ray topography analyses show that the overall quality of the crystals prepared in the presence of this cryoprotectant is enhanced. Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.,Charron C, Kadri A, Robert MC, Giege R, Lorber B Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2060-5. Epub 2002, Nov 23. PMID:12454465 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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