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| | ==Structure of FAE solved by SAD from data collected by Direct Data Collection (DDC) using the ESRF RoboDiff goniometer== | | ==Structure of FAE solved by SAD from data collected by Direct Data Collection (DDC) using the ESRF RoboDiff goniometer== |
| - | <StructureSection load='5fxm' size='340' side='right' caption='[[5fxm]], [[Resolution|resolution]] 1.99Å' scene=''> | + | <StructureSection load='5fxm' size='340' side='right'caption='[[5fxm]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fxm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FXM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fxm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FXM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fxl|5fxl]], [[5fxn|5fxn]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxm OCA], [https://pdbe.org/5fxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fxm RCSB], [https://www.ebi.ac.uk/pdbsum/5fxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxm ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Feruloyl_esterase Feruloyl esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.73 3.1.1.73] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fxm OCA], [http://pdbe.org/5fxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fxm RCSB], [http://www.ebi.ac.uk/pdbsum/5fxm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fxm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Feruloyl esterase]] | + | [[Category: Acetivibrio thermocellus]] |
| - | [[Category: Bowler, M W]] | + | [[Category: Large Structures]] |
| - | [[Category: Nurizzo, D]] | + | [[Category: Bowler MW]] |
| - | [[Category: Hydrolase]] | + | [[Category: Nurizzo D]] |
| Structural highlights
Publication Abstract from PubMed
Automation of the mounting of cryocooled samples is now a feature of the majority of beamlines dedicated to macromolecular crystallography (MX). Robotic sample changers have been developed over many years, with the latest designs increasing capacity, reliability and speed. Here, the development of a new sample changer deployed at the ESRF beamline MASSIF-1 (ID30A-1), based on an industrial six-axis robot, is described. The device, named RoboDiff, includes a high-capacity dewar, acts as both a sample changer and a high-accuracy goniometer, and has been designed for completely unattended sample mounting and diffraction data collection. This aim has been achieved using a high level of diagnostics at all steps of the process from mounting and characterization to data collection. The RoboDiff has been in service on the fully automated endstation MASSIF-1 at the ESRF since September 2014 and, at the time of writing, has processed more than 20 000 samples completely automatically.
RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments.,Nurizzo D, Bowler MW, Caserotto H, Dobias F, Giraud T, Surr J, Guichard N, Papp G, Guijarro M, Mueller-Dieckmann C, Flot D, McSweeney S, Cipriani F, Theveneau P, Leonard GA Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):966-75. doi:, 10.1107/S205979831601158X. Epub 2016 Jul 27. PMID:27487827[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nurizzo D, Bowler MW, Caserotto H, Dobias F, Giraud T, Surr J, Guichard N, Papp G, Guijarro M, Mueller-Dieckmann C, Flot D, McSweeney S, Cipriani F, Theveneau P, Leonard GA. RoboDiff: combining a sample changer and goniometer for highly automated macromolecular crystallography experiments. Acta Crystallogr D Struct Biol. 2016 Aug;72(Pt 8):966-75. doi:, 10.1107/S205979831601158X. Epub 2016 Jul 27. PMID:27487827 doi:http://dx.doi.org/10.1107/S205979831601158X
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