4h35

Feruloyl Esterase Domain of XYNY from Clostridium thermocellum before exposure to 266nm UV laser

spinqualitylabelsall models 4h35, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h35 is a 2 chain structure with sequence from Acetivibrio thermocellus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CD, MSE, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function XYNY_ACETH Publication Abstract from PubMed Selenomethionine labeling is the most common technique used in protein crystallography to derivatize recombinant proteins for experimental phasing using anomalous scattering at tunable synchrotron beamlines. Recently, it has been shown that UV radiation depletes electron density of selenium atoms of selenomethionine residues and that UV radiation- damage induced phasing (equivalent to single isomorphous replacement) protocol can be applied to calculate experimental phases. Here we present the straightforward integration of a UV source with an in-house diffractometer. We show how this setup can extend the capabilities of a sealed tube X-ray generator and be used for experimental phasing of selenium-labeled proteins. In-house UV radiation damage induced phasing of selenomethionine-labeled protein structures.,Pereira PJ, Royant A, Panjikar S, de Sanctis D J Struct Biol. 2012 Nov 20. pii: S1047-8477(12)00315-2. doi:, 10.1016/j.jsb.2012.11.003. PMID:23178456 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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