6fj2

Structure of Thermolysin solved from SAD data collected at the peak of the Zn absorption edge on ID30B

spinqualitylabelsall models 6fj2, resolution 1.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fj2 is a 1 chain structure with sequence from 'bacillus thermoproteolyticus'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, DMS, LYS, TMO, VAL, ZN Related: 6fid Gene: npr ('Bacillus thermoproteolyticus') Activity: Thermolysin, with EC number 3.4.24.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [THER_BACTH] Extracellular zinc metalloprotease. Publication Abstract from PubMed ID30B is an undulator-based high-intensity, energy-tuneable (6.0-20 keV) and variable-focus (20-200 microm in diameter) macromolecular crystallography (MX) beamline at the ESRF. It was the last of the ESRF Structural Biology Group's beamlines to be constructed and commissioned as part of the ESRF's Phase I Upgrade Program and has been in user operation since June 2015. Both a modified microdiffractometer (MD2S) incorporating an in situ plate screening capability and a new flexible sample changer (the FlexHCD) were specifically developed for ID30B. Here, the authors provide the current beamline characteristics and detail how different types of MX experiments can be performed on ID30B (https://www.esrf.eu/id30b). ID30B - a versatile beamline for macromolecular crystallography experiments at the ESRF.,McCarthy AA, Barrett R, Beteva A, Caserotto H, Dobias F, Felisaz F, Giraud T, Guijarro M, Janocha R, Khadrouche A, Lentini M, Leonard GA, Lopez Marrero M, Malbet-Monaco S, McSweeney S, Nurizzo D, Papp G, Rossi C, Sinoir J, Sorez C, Surr J, Svensson O, Zander U, Cipriani F, Theveneau P, Mueller-Dieckmann C J Synchrotron Radiat. 2018 Jul 1;25(Pt 4):1249-1260. doi:, 10.1107/S1600577518007166. Epub 2018 Jun 27. PMID:29979188 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thermolysin

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