2oqn

High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths

spinqualitylabelsall models 2oqn, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2oqn 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 1.9Å Ligands: TAR 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 Crystal cryocooling is usually employed to reduce radiation damage during X-ray crystallography. Recently, a high-pressure cryocooling method has been developed which results in excellent diffraction-quality crystals without the use of penetrative cryoprotectants. Three new developments of the method are presented here: (i) Xe-He high-pressure cryocooling for Xe SAD phasing, (ii) native sulfur SAD phasing and (iii) successful cryopreservation of crystals in thick-walled capillaries without additional cryoprotectants other than the native mother liquor. These developments may be useful for structural solution of proteins without the need for selenomethionine incorporation and for high-throughput protein crystallography. High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths.,Kim CU, Hao Q, Gruner SM Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):653-9. Epub 2007, Apr 21. PMID:17452791 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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