4c3c

Thaumatin refined against hatrx data for time-point 1Thaumatin refined against hatrx data for time-point 1

Structural highlights 4c3c 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 1.8Å Ligands: 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 We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy. Time-resolved crystallography using the Hadamard transform.,Yorke BA, Beddard GS, Owen RL, Pearson AR Nat Methods. 2014 Nov;11(11):1131-4. doi: 10.1038/nmeth.3139. Epub 2014 Oct 5. PMID:25282611 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 4c3c, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image