2jic

High resolution structure of xylanase-II from one micron beam experiment

spinqualitylabelsall models 2jic, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jic is a 1 chain structure with sequence from Trichoderma longibrachiatum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F8W669_TRILO 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 For the first time, protein microcrystallography has been performed with a focused synchrotron-radiation beam of 1 microm using a goniometer with a sub-micrometre sphere of confusion. The crystal structure of xylanase II has been determined with a flux density of about 3 x 10(10) photons s(-1) microm(-2) at the sample. Two sets of diffraction images collected from different sized crystals were shown to comprise data of good quality, which allowed a 1.5 A resolution xylanase II structure to be obtained. The main conclusion of this experiment is that a high-resolution diffraction pattern can be obtained from 20 microm(3) crystal volume, corresponding to about 2 x 10(8) unit cells. Despite the high irradiation dose in this case, it was possible to obtain an excellent high-resolution map and it could be concluded from the individual atomic B-factor patterns that there was no evidence of significant radiation damage. The photoelectron escape from a narrow diffraction channel is a possible reason for reduced radiation damage as indicated by Monte Carlo simulations. These results open many new opportunities in scanning protein microcrystallography and make random data collection from microcrystals a real possibility, therefore enabling structures to be solved from much smaller crystals than previously anticipated as long as the crystallites are well ordered. Protein crystallography with a micrometre-sized synchrotron-radiation beam.,Moukhametzianov R, Burghammer M, Edwards PC, Petitdemange S, Popov D, Fransen M, McMullan G, Schertler GF, Riekel C Acta Crystallogr D Biol Crystallogr. 2008 Feb;64(Pt 2):158-66. Epub 2008, Jan 16. PMID:18219115 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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