7a44: Difference between revisions
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==CO-bound sperm whale myoglobin measured by serial synchrotron crystallography== | ==CO-bound sperm whale myoglobin measured by serial synchrotron crystallography== | ||
<StructureSection load='7a44' size='340' side='right'caption='[[7a44]]' scene=''> | <StructureSection load='7a44' size='340' side='right'caption='[[7a44]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A44 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7a44]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A44 FirstGlance]. <br> | ||
</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=7a44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a44 OCA], [https://pdbe.org/7a44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a44 RCSB], [https://www.ebi.ac.uk/pdbsum/7a44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a44 ProSAT]</span></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]] 1.75Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7a44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a44 OCA], [https://pdbe.org/7a44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a44 RCSB], [https://www.ebi.ac.uk/pdbsum/7a44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a44 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution. | |||
Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.,Mehrabi P, Bucker R, Bourenkov G, Ginn HM, von Stetten D, Muller-Werkmeister HM, Kuo A, Morizumi T, Eger BT, Ou WL, Oghbaey S, Sarracini A, Besaw JE, Pare-Labrosse O, Meier S, Schikora H, Tellkamp F, Marx A, Sherrell DA, Axford D, Owen RL, Ernst OP, Pai EF, Schulz EC, Miller RJD Sci Adv. 2021 Mar 17;7(12). pii: 7/12/eabf1380. doi: 10.1126/sciadv.abf1380., Print 2021 Mar. PMID:33731353<ref>PMID:33731353</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7a44" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Myoglobin 3D structures|Myoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Physeter catodon]] | |||
[[Category: Buecker R]] | [[Category: Buecker R]] | ||
[[Category: Mehrabi P]] | [[Category: Mehrabi P]] | ||
[[Category: Schulz EC]] | [[Category: Schulz EC]] | ||
Latest revision as of 15:03, 1 February 2024
CO-bound sperm whale myoglobin measured by serial synchrotron crystallographyCO-bound sperm whale myoglobin measured by serial synchrotron crystallography
Structural highlights
FunctionMYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMedFor the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution. Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.,Mehrabi P, Bucker R, Bourenkov G, Ginn HM, von Stetten D, Muller-Werkmeister HM, Kuo A, Morizumi T, Eger BT, Ou WL, Oghbaey S, Sarracini A, Besaw JE, Pare-Labrosse O, Meier S, Schikora H, Tellkamp F, Marx A, Sherrell DA, Axford D, Owen RL, Ernst OP, Pai EF, Schulz EC, Miller RJD Sci Adv. 2021 Mar 17;7(12). pii: 7/12/eabf1380. doi: 10.1126/sciadv.abf1380., Print 2021 Mar. PMID:33731353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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