7o7d - Revision history

OCA at 12:46, 1 February 2024

2024-02-01T12:46:05Z

←Older revision		Revision as of 12:46, 1 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7o7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[7o7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</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]] 1.4Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 7o7d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 7o7d" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Green Fluorescent Protein 3D structures\|Green Fluorescent Protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:30, 19 October 2022

2022-10-19T19:30:10Z

←Older revision		Revision as of 19:30, 19 October 2022
Line 8:		Line 8:
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.	+	[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 04:07, 8 September 2022

2022-09-08T04:07:52Z

←Older revision		Revision as of 04:07, 8 September 2022
Line 1:		Line 1:

	==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==		==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==
-	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]]' scene=''>	+	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]], [[Resolution\|resolution]] 1.40Å' 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=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7o7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D 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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Reversibly photoswitchable fluorescent proteins are essential markers for advanced biological imaging, and optimization of their photophysical properties underlies improved performance and novel applications. Here we establish a link between photoswitching contrast, one of the key parameters that dictate the achievable resolution in nanoscopy applications, and chromophore conformation in the non-fluorescent state of rsEGFP2, a widely employed label in REversible Saturable OpticaL Fluorescence Transitions (RESOLFT) microscopy. Upon illumination, the cis chromophore of rsEGFP2 isomerizes to two distinct off-state conformations, trans1 and trans2, located on either side of the V151 side chain. Reducing or enlarging the side chain at this position (V151A and V151L variants) leads to single off-state conformations that exhibit higher and lower switching contrast, respectively, compared to the rsEGFP2 parent. The combination of structural information obtained by serial femtosecond crystallography with high-level quantum chemical calculations and with spectroscopic and photophysical data determined in vitro suggests that the changes in switching contrast arise from blue- and red-shifts of the absorption bands associated to trans1 and trans2, respectively. Thus, due to elimination of trans2, the V151A variants of rsEGFP2 and its superfolding variant rsFolder2 display a more than two-fold higher switching contrast than their respective parent proteins, both in vitro and in E. coli cells. The application of the rsFolder2-V151A variant is demonstrated in RESOLFT nanoscopy. Our study rationalizes the connection between structural and photophysical chromophore properties and suggests a means to rationally improve fluorescent proteins for nanoscopy applications.
		+
		+	Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement.,Adam V, Hadjidemetriou K, Jensen N, Shoeman RL, Woodhouse J, Aquila A, Banneville AS, Barends TRM, Bezchastnov V, Boutet S, Byrdin M, Cammarata M, Carbajo S, Eleni Christou N, Coquelle N, De la Mora E, El Khatib M, Moreno Chicano T, Bruce Doak R, Fieschi F, Foucar L, Glushonkov O, Gorel A, Grunbein ML, Hilpert M, Hunter M, Kloos M, Koglin JE, Lane TJ, Liang M, Mantovanelli A, Nass K, Nass Kovacs G, Owada S, Roome CM, Schiro G, Seaberg M, Stricker M, Thepaut M, Tono K, Ueda K, Uriarte LM, You D, Zala N, Domratcheva T, Jakobs S, Sliwa M, Schlichting I, Colletier JP, Bourgeois D, Weik M Chemphyschem. 2022 Aug 12:e202200192. doi: 10.1002/cphc.202200192. PMID:35959919<ref>PMID:35959919</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7o7d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aequorea victoria]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Adam V]]		[[Category: Adam V]]

OCA at 11:03, 31 August 2022

2022-08-31T11:03:55Z

←Older revision		Revision as of 11:03, 31 August 2022
Line 1:		Line 1:

	==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==		==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==
-	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]]~~, [[Resolution\|resolution]] 1.40Å~~' scene=''>	+	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[7o7d]] is a 1 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>
-	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</scene></td></tr>	+	</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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Reversibly photoswitchable fluorescent proteins are essential markers for advanced biological imaging, and optimization of their photophysical properties underlies improved performance and novel applications. Here we establish a link between photoswitching contrast, one of the key parameters that dictate the achievable resolution in nanoscopy applications, and chromophore conformation in the non-fluorescent state of rsEGFP2, a widely employed label in REversible Saturable OpticaL Fluorescence Transitions (RESOLFT) microscopy. Upon illumination, the cis chromophore of rsEGFP2 isomerizes to two distinct off-state conformations, trans1 and trans2, located on either side of the V151 side chain. Reducing or enlarging the side chain at this position (V151A and V151L variants) leads to single off-state conformations that exhibit higher and lower switching contrast, respectively, compared to the rsEGFP2 parent. The combination of structural information obtained by serial femtosecond crystallography with high-level quantum chemical calculations and with spectroscopic and photophysical data determined in vitro suggests that the changes in switching contrast arise from blue- and red-shifts of the absorption bands associated to trans1 and trans2, respectively. Thus, due to elimination of trans2, the V151A variants of rsEGFP2 and its superfolding variant rsFolder2 display a more than two-fold higher switching contrast than their respective parent proteins, both in vitro and in E. coli cells. The application of the rsFolder2-V151A variant is demonstrated in RESOLFT nanoscopy. Our study rationalizes the connection between structural and photophysical chromophore properties and suggests a means to rationally improve fluorescent proteins for nanoscopy applications.
-
-	Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement.,Adam V, Hadjidemetriou K, Jensen N, Shoeman RL, Woodhouse J, Aquila A, Banneville AS, Barends TRM, Bezchastnov V, Boutet S, Byrdin M, Cammarata M, Carbajo S, Eleni Christou N, Coquelle N, De la Mora E, El Khatib M, Moreno Chicano T, Bruce Doak R, Fieschi F, Foucar L, Glushonkov O, Gorel A, Grunbein ML, Hilpert M, Hunter M, Kloos M, Koglin JE, Lane TJ, Liang M, Mantovanelli A, Nass K, Nass Kovacs G, Owada S, Roome CM, Schiro G, Seaberg M, Stricker M, Thepaut M, Tono K, Ueda K, Uriarte LM, You D, Zala N, Domratcheva T, Jakobs S, Sliwa M, Schlichting I, Colletier JP, Bourgeois D, Weik M Chemphyschem. 2022 Aug 12:e202200192. doi: 10.1002/cphc.202200192. PMID:35959919<ref>PMID:35959919</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7o7d" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Adam, V]]	+	[[Category: Adam V]]
-	[[Category: Colletier, J P]]	+	[[Category: Colletier J-P]]
-	[[Category: Hadjidemetriou, K]]	+	[[Category: Hadjidemetriou K]]
-	[[Category: Weik, M]]	+	[[Category: Weik M]]
-	[[Category: Woodhouse, J]]	+	[[Category: Woodhouse J]]
-	~~[[Category: Fluorescent protein]]~~	+
-	~~[[Category: Reversibly photoswitchable fluorescent protein~~]]	+

OCA at 05:11, 25 August 2022

2022-08-25T05:11:37Z

←Older revision		Revision as of 05:11, 25 August 2022
Line 1:		Line 1:

	==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==		==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==
-	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]]' scene=''>	+	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]], [[Resolution\|resolution]] 1.40Å' 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=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7o7d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D 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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Reversibly photoswitchable fluorescent proteins are essential markers for advanced biological imaging, and optimization of their photophysical properties underlies improved performance and novel applications. Here we establish a link between photoswitching contrast, one of the key parameters that dictate the achievable resolution in nanoscopy applications, and chromophore conformation in the non-fluorescent state of rsEGFP2, a widely employed label in REversible Saturable OpticaL Fluorescence Transitions (RESOLFT) microscopy. Upon illumination, the cis chromophore of rsEGFP2 isomerizes to two distinct off-state conformations, trans1 and trans2, located on either side of the V151 side chain. Reducing or enlarging the side chain at this position (V151A and V151L variants) leads to single off-state conformations that exhibit higher and lower switching contrast, respectively, compared to the rsEGFP2 parent. The combination of structural information obtained by serial femtosecond crystallography with high-level quantum chemical calculations and with spectroscopic and photophysical data determined in vitro suggests that the changes in switching contrast arise from blue- and red-shifts of the absorption bands associated to trans1 and trans2, respectively. Thus, due to elimination of trans2, the V151A variants of rsEGFP2 and its superfolding variant rsFolder2 display a more than two-fold higher switching contrast than their respective parent proteins, both in vitro and in E. coli cells. The application of the rsFolder2-V151A variant is demonstrated in RESOLFT nanoscopy. Our study rationalizes the connection between structural and photophysical chromophore properties and suggests a means to rationally improve fluorescent proteins for nanoscopy applications.
		+
		+	Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement.,Adam V, Hadjidemetriou K, Jensen N, Shoeman RL, Woodhouse J, Aquila A, Banneville AS, Barends TRM, Bezchastnov V, Boutet S, Byrdin M, Cammarata M, Carbajo S, Eleni Christou N, Coquelle N, De la Mora E, El Khatib M, Moreno Chicano T, Bruce Doak R, Fieschi F, Foucar L, Glushonkov O, Gorel A, Grunbein ML, Hilpert M, Hunter M, Kloos M, Koglin JE, Lane TJ, Liang M, Mantovanelli A, Nass K, Nass Kovacs G, Owada S, Roome CM, Schiro G, Seaberg M, Stricker M, Thepaut M, Tono K, Ueda K, Uriarte LM, You D, Zala N, Domratcheva T, Jakobs S, Sliwa M, Schlichting I, Colletier JP, Bourgeois D, Weik M Chemphyschem. 2022 Aug 12:e202200192. doi: 10.1002/cphc.202200192. PMID:35959919<ref>PMID:35959919</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7o7d" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Adam V]]	+	[[Category: Adam, V]]
-	[[Category: Colletier J-P]]	+	[[Category: Colletier, J P]]
-	[[Category: Hadjidemetriou K]]	+	[[Category: Hadjidemetriou, K]]
-	[[Category: Weik M]]	+	[[Category: Weik, M]]
-	[[Category: Woodhouse J]]	+	[[Category: Woodhouse, J]]
		+	[[Category: Fluorescent protein]]
		+	[[Category: Reversibly photoswitchable fluorescent protein]]

OCA at 18:00, 27 July 2022

2022-07-27T18:00:28Z

←Older revision		Revision as of 18:00, 27 July 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 7o7d is ON HOLD until Paper Publication~~	+	==Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K==
-		+	<StructureSection load='7o7d' size='340' side='right'caption='[[7o7d]]' scene=''>
-	~~Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O7D FirstGlance]. <br>
-	~~Description:~~ Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K	+	</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=7o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o7d OCA], [https://pdbe.org/7o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o7d RCSB], [https://www.ebi.ac.uk/pdbsum/7o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o7d ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Adam~~, V]]	+	__TOC__
-	[[Category: ~~Hadjidemetriou, K~~]]	+	</StructureSection>
-	[[Category: ~~Woodhouse, J~~]]	+	[[Category: Large Structures]]
-	[[Category: Colletier, J.-P]]	+	[[Category: Adam V]]
-	[[Category: Weik, M]]	+	[[Category: Colletier J-P]]
		+	[[Category: Hadjidemetriou K]]
		+	[[Category: Weik M]]
		+	[[Category: Woodhouse J]]

OCA at 08:20, 12 May 2021

2021-05-12T08:20:35Z

←Older revision		Revision as of 08:20, 12 May 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7o7d is ON HOLD	+	The entry 7o7d is ON HOLD until Paper Publication

	Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M.		Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M.

OCA: Protected "7o7d" [edit=sysop:move=sysop]

2021-04-21T06:40:36Z

Protected "7o7d" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:40, 21 April 2021

OCA: New page: '''Unreleased structure''' The entry 7o7d is ON HOLD Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M. Description: Crystal structure of rsEGFP2 mutant V...

2021-04-21T06:40:34Z

New page: '''Unreleased structure''' The entry 7o7d is ON HOLD Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M. Description: Crystal structure of rsEGFP2 mutant V...

New page

'''Unreleased structure'''

The entry 7o7d is ON HOLD

Authors: Woodhouse, J., Adam, V., Hadjidemetriou, K., Colletier, J.-P., Weik, M.

Description: Crystal structure of rsEGFP2 mutant V151A in the fluorescent on-state determined by synchrotron radiation at 100K
[[Category: Unreleased Structures]]
[[Category: Adam, V]]
[[Category: Hadjidemetriou, K]]
[[Category: Woodhouse, J]]
[[Category: Colletier, J.-P]]
[[Category: Weik, M]]