5oqe: Difference between revisions
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<StructureSection load='5oqe' size='340' side='right'caption='[[5oqe]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='5oqe' size='340' side='right'caption='[[5oqe]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oqe]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5oqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lobophyllia_hemprichii Lobophyllia hemprichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OQE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=VYA:2-[(4~{Z})-2-[(1~{S})-1-azanyl-3-methyl-butyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxidanylidene-imidazol-1-yl]ethanoic+acid'>VYA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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=5oqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oqe OCA], [https://pdbe.org/5oqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oqe RCSB], [https://www.ebi.ac.uk/pdbsum/5oqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oqe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5S6Z9_LOBHE Q5S6Z9_LOBHE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lobophyllia hemprichii]] | ||
[[Category: Cordon-Preciado | [[Category: Cordon-Preciado V]] | ||
[[Category: Hutchison | [[Category: Hutchison CDM]] | ||
[[Category: Morgan | [[Category: Morgan RML]] | ||
[[Category: Thor | [[Category: Van Thor JJ]] | ||
Latest revision as of 12:53, 15 November 2023
XFEL structure of the on state of a reversibly photoswitching fluorescent protein determined using the droplet injection methodXFEL structure of the on state of a reversibly photoswitching fluorescent protein determined using the droplet injection method
Structural highlights
FunctionPublication Abstract from PubMedThe photochromic fluorescent protein Skylan-NS (Nonlinear Structured illumination variant mEos3.1H62L) is a reversibly photoswitchable fluorescent protein which has an unilluminated/ground state with an anionic and cis chromophore conformation and high fluorescence quantum yield. Photo-conversion with illumination at 515 nm generates a meta-stable intermediate with neutral trans-chromophore structure that has a 4 h lifetime. We present X-ray crystal structures of the cis (on) state at 1.9 Angstrom resolution and the trans (off) state at a limiting resolution of 1.55 Angstrom from serial femtosecond crystallography experiments conducted at SPring-8 Angstrom Compact Free Electron Laser (SACLA) at 7.0 keV and 10.5 keV, and at Linac Coherent Light Source (LCLS) at 9.5 keV. We present a comparison of the data reduction and structure determination statistics for the two facilities which differ in flux, beam characteristics and detector technologies. Furthermore, a comparison of droplet on demand, grease injection and Gas Dynamic Virtual Nozzle (GDVN) injection shows no significant differences in limiting resolution. The photoconversion of the on- to the off-state includes both internal and surface exposed protein structural changes, occurring in regions that lack crystal contacts in the orthorhombic crystal form. X-ray Free Electron Laser Determination of Crystal Structures of Dark and Light States of a Reversibly Photoswitching Fluorescent Protein at Room Temperature.,Hutchison CDM, Cordon-Preciado V, Morgan RML, Nakane T, Ferreira J, Dorlhiac G, Sanchez-Gonzalez A, Johnson AS, Fitzpatrick A, Fare C, Marangos JP, Yoon CH, Hunter MS, DePonte DP, Boutet S, Owada S, Tanaka R, Tono K, Iwata S, van Thor JJ Int J Mol Sci. 2017 Sep 7;18(9). pii: ijms18091918. doi: 10.3390/ijms18091918. PMID:28880248[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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