8cl8: Difference between revisions
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==Krokinobacter eikastus rhodopsin 2 (KR2) extrapolated map 1us after light activation== | |||
<StructureSection load='8cl8' size='340' side='right'caption='[[8cl8]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dokdonia_eikasta Dokdonia eikasta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CL8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=8cl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cl8 OCA], [https://pdbe.org/8cl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cl8 RCSB], [https://www.ebi.ac.uk/pdbsum/8cl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cl8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/N0DKS8_9FLAO N0DKS8_9FLAO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced. In-built temperature control of samples facilitated optimal extrusion and supported sample stability. After commissioning the device with lysozyme crystals, we collected time-resolved data using crystals of a membrane-bound, light-driven sodium pump. Static data were also collected from the soluble protein tubulin that was soaked with a series of small molecule drugs. Using these data, we identify low occupancy (as little as 30%) ligands using a minimal amount of data from a serial crystallography experiment, a result that could be exploited for structure-based drug design. | |||
A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.,Wranik M, Kepa MW, Beale EV, James D, Bertrand Q, Weinert T, Furrer A, Glover H, Gashi D, Carrillo M, Kondo Y, Stipp RT, Khusainov G, Nass K, Ozerov D, Cirelli C, Johnson PJM, Dworkowski F, Beale JH, Stubbs S, Zamofing T, Schneider M, Krauskopf K, Gao L, Thorn-Seshold O, Bostedt C, Bacellar C, Steinmetz MO, Milne C, Standfuss J Nat Commun. 2023 Dec 2;14(1):7956. doi: 10.1038/s41467-023-43523-5. PMID:38042952<ref>PMID:38042952</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bertrand | <div class="pdbe-citations 8cl8" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Weinert | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Dokdonia eikasta]] | |||
[[Category: Large Structures]] | |||
[[Category: Bertrand Q]] | |||
[[Category: Kepa MW]] | |||
[[Category: Standfuss J]] | |||
[[Category: Weinert T]] | |||
[[Category: Wranik M]] | |||
Latest revision as of 14:39, 13 December 2023
Krokinobacter eikastus rhodopsin 2 (KR2) extrapolated map 1us after light activationKrokinobacter eikastus rhodopsin 2 (KR2) extrapolated map 1us after light activation
Structural highlights
FunctionPublication Abstract from PubMedSerial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced. In-built temperature control of samples facilitated optimal extrusion and supported sample stability. After commissioning the device with lysozyme crystals, we collected time-resolved data using crystals of a membrane-bound, light-driven sodium pump. Static data were also collected from the soluble protein tubulin that was soaked with a series of small molecule drugs. Using these data, we identify low occupancy (as little as 30%) ligands using a minimal amount of data from a serial crystallography experiment, a result that could be exploited for structure-based drug design. A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.,Wranik M, Kepa MW, Beale EV, James D, Bertrand Q, Weinert T, Furrer A, Glover H, Gashi D, Carrillo M, Kondo Y, Stipp RT, Khusainov G, Nass K, Ozerov D, Cirelli C, Johnson PJM, Dworkowski F, Beale JH, Stubbs S, Zamofing T, Schneider M, Krauskopf K, Gao L, Thorn-Seshold O, Bostedt C, Bacellar C, Steinmetz MO, Milne C, Standfuss J Nat Commun. 2023 Dec 2;14(1):7956. doi: 10.1038/s41467-023-43523-5. PMID:38042952[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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