3zi6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of thermolysin solved by SAD from data collected by Direct Data Collection (DDC) using the GRob robot goniometer== | ==Structure of thermolysin solved by SAD from data collected by Direct Data Collection (DDC) using the GRob robot goniometer== | ||
<StructureSection load='3zi6' size='340' side='right' caption='[[3zi6]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3zi6' size='340' side='right' caption='[[3zi6]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| Line 6: | Line 7: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zi7|3zi7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zi7|3zi7]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </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=3zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zi6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zi6 PDBsum]</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=3zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zi6 OCA], [http://pdbe.org/3zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zi6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zi6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 10:38, 5 August 2016
Structure of thermolysin solved by SAD from data collected by Direct Data Collection (DDC) using the GRob robot goniometerStructure of thermolysin solved by SAD from data collected by Direct Data Collection (DDC) using the GRob robot goniometer
Structural highlights
Function[THER_BACTH] Extracellular zinc metalloprotease. Publication Abstract from PubMedIntroduction: X-ray crystallography is the main tool for macromolecular structure solution at atomic resolution. It provides key information for the understanding of protein function, opening opportunities for the modulation of enzymatic mechanisms, and protein-ligand interactions. As a consequence, macromolecular crystallography plays an essential role in drug design, as well as in the a posteriori validation of drug mechanisms. Areas covered: The demand for method developments and also tools for macromolecular crystallography has significantly increased over the past 10 years. As a consequence, access to the facilities required for these investigations, such as synchrotron beamlines, became more difficult and significant efforts were dedicated to the automation of the experimental setup in laboratories. In this article, the authors describe how this was accomplished and how robot-based systems contribute to the enhancement of the macromolecular structure solution pipeline. Expert opinion: The evolution in robot technology, together with progress in X-ray beam performance and software developments, contributes to a new era in macromolecular X-ray crystallography. Highly integrated experimental environments open new possibilities for crystallography experiments. It is likely that it will also change the way this technique will be used in the future, opening the field to a larger community. Recent progress in robot-based systems for crystallography and their contribution to drug discovery.,Ferrer JL, Larive NA, Bowler MW, Nurizzo D Expert Opin Drug Discov. 2013 May 8. PMID:23656378[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||