2jic
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==High resolution structure of xylanase-II from one micron beam experiment== | ==High resolution structure of xylanase-II from one micron beam experiment== | ||
| - | <StructureSection load='2jic' size='340' side='right' caption='[[2jic]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='2jic' size='340' side='right'caption='[[2jic]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2jic]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2jic]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_longibrachiatum Trichoderma longibrachiatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JIC FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jic OCA], [https://pdbe.org/2jic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jic RCSB], [https://www.ebi.ac.uk/pdbsum/2jic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jic ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F8W669_TRILO F8W669_TRILO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2jic_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2jic_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jic ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
| Line 20: | Line 25: | ||
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<ref>PMID:18219115</ref> | 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<ref>PMID:18219115</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2jic" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
[[Category: Trichoderma longibrachiatum]] | [[Category: Trichoderma longibrachiatum]] | ||
| - | [[Category: Burghammer | + | [[Category: Burghammer M]] |
| - | [[Category: Edwards | + | [[Category: Edwards PC]] |
| - | [[Category: Fransen | + | [[Category: Fransen M]] |
| - | [[Category: Moukhametzianov | + | [[Category: Moukhametzianov R]] |
| - | [[Category: Petitdemange | + | [[Category: Petitdemange S]] |
| - | [[Category: Popov | + | [[Category: Popov D]] |
| - | [[Category: Riekel | + | [[Category: Riekel C]] |
| - | [[Category: Schertler | + | [[Category: Schertler GF]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
High resolution structure of xylanase-II from one micron beam experiment
| |||||||||||
