1dwf | pdb_00001dwf

STUDY ON RADIATION DAMAGE ON A CRYOCOOLED CRYSTAL. PART 2: STRUCTURE AFTER IRRADIATION WITH 9.1*10E15 PHOTONS/MM2

spinqualitylabelsall models 1dwf, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dwf is a 1 chain structure with sequence from Sinapis alba. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, GOL, NAG, SO4, ZN, FUC, MAN, XYP Related: 1myr, 1dwa, 1dwg, 1dwh, 1dwi, 1dwj Activity: Thioglucosidase, with EC number 3.2.1.147 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [MYRA_SINAL] Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. 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 high intensity of third-generation X-ray sources, along with the development of cryo-cooling of protein crystals at temperatures around 100 K, have made it possible to extend the diffraction limit of crystals and to reduce their size. However, even with cryo-cooled crystals, radiation damage becomes a limiting factor. So far, the radiation damage has manifested itself in the form of a loss of overall diffracted intensity and an increase in the temperature factor. The structure of a protein (myrosinase) after exposure to different doses of X-rays in the region of 20 x 10(15) photons mm(-2) has been studied. The changes in the structure owing to radiation damage were analysed using Fourier difference maps and occupancy refinement for the first time. Damage was obvious in the form of breakage of disulfide bonds, decarboxylation of aspartate and glutamate residues, a loss of hydroxyl groups from tyrosine and of the methylthio group of methionine. The susceptibility to radiation damage of individual groups of the same kind varies within the protein. The quality of the model resulting from structure determination might be compromised owing to the presence of radiolysis in the crystal after an excessive radiation dose. Radiation-induced structural changes may interfere with the interpretation of ligand-binding studies or MAD data. The experiments reported here suggest that there is an intrinsic limit to the amount of data which can be extracted from a sample of a given size. Structural changes in a cryo-cooled protein crystal owing to radiation damage.,Burmeister WP Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):328-41. PMID:10713520 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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