5df5 - Revision history

OCA at 11:26, 10 January 2024

OCA — Wed, 10 Jan 2024 11:26:03 GMT

←Older revision		Revision as of 11:26, 10 January 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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]] 1.301Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [https://pdbe.org/5df5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [https://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [https://pdbe.org/5df5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [https://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 10:32, 21 June 2023

OCA — Wed, 21 Jun 2023 10:32:54 GMT

←Older revision		Revision as of 10:32, 21 June 2023
Line 1:		Line 1:

	==The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.==		==The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.==
-	<StructureSection load='5df5' size='340' side='right' caption='[[5df5]], [[Resolution\|resolution]] 1.30Å' scene=''>	+	<StructureSection load='5df5' size='340' side='right'caption='[[5df5]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c0z\|5c0z]]</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [https://pdbe.org/5df5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [https://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cycs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])~~</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [~~http~~://pdbe.org/5df5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CYC_RAT CYC_RAT]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).	+	[https://www.uniprot.org/uniprot/CYC_RAT CYC_RAT] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Mammalian cytochrome c (Cytc) transfers electrons from the bc(1) complex to cytochrome c oxidase (CcO) as part of the mitochondrial electron transport chain, and it also participates in type II apoptosis. Our recent discovery of two tyrosine phosphorylation sites in Cytc, Tyr97 in bovine heart and Tyr48 in bovine liver, indicates that Cytc functions are regulated through cell signaling. To characterize the role of Cytc tyrosine phosphorylation in detail using an independent approach, we here overexpressed and purified a Tyr48Glu mutant Cytc, mimicking the in vivo Tyr48 phosphorylation found in cow liver, along with wild-type and Tyr48Phe variants as controls. The midpoint redox potential of the phosphomimetic mutant was decreased by 45 mV compared to control (192 vs 237 mV). Similar to Tyr48 in vivo phosphorylated Cytc, direct kinetic analysis of the Cytc reaction with isolated CcO revealed decreased V(max) for the Tyr48Glu mutant by 30% compared to wild type or the Tyr48Phe variants. Moreover, the phosphomimetic substitution resulted in major changes of Cytc functions related to apoptosis. The binding affinity of Tyr48Glu Cytc to cardiolipin was decreased by about 30% compared to wild type or the Tyr48Phe variants, and Cytc peroxidase activity of the Tyr48Glu mutant was cardiolipin-inducible only at high cardiolipin concentration, unlike controls. Importantly, the Tyr48Glu Cytc failed to induce any detectable downstream activation of caspase-3. Our data suggest that in vivo Tyr48 phosphorylation might serve as an antiapoptotic switch and highlight the strategic position and role of the conserved Cytc residue Tyr48 in regulating multiple functions of Cytc.	+

-	Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation.,Pecina P, Borisenko GG, Belikova NA, Tyurina YY, Pecinova A, Lee I, Samhan-Arias AK, Przyklenk K, Kagan VE, Huttemann M Biochemistry. 2010 Aug 10;49(31):6705-14. doi: 10.1021/bi100486s. PMID:20586425<ref>PMID:20586425</ref>	+	==See Also==
-		+	*[[Cytochrome C 3D structures\|Cytochrome C 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 5df5" style~~=~~"background-color:#fffaf0;"></div>~~	+
-	~~== References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Large Structures]]
-	[[Category: Brunzelle~~, J S~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Edwards~~, B F.P~~]]	+	[[Category: Brunzelle JS]]
-	[[Category: Huttemann, M]]	+	[[Category: Edwards BFP]]
-	[[Category: Mahapatra, G]]	+	[[Category: Huttemann M]]
-	[[Category: Vaishnav~~, A A]]~~	+	[[Category: Mahapatra G]]
-	~~[[Category: Cytochrome c]]~~	+	[[Category: Vaishnav AA]]
-	~~[[Category: Electron transport]]~~	+
-	~~[[Category: Mutant]]~~	+
-	~~[[Category: Oxidized]]~~	+
-	~~[[Category: Rat~~]]	+

OCA at 06:51, 31 January 2018

OCA — Wed, 31 Jan 2018 06:51:55 GMT

←Older revision		Revision as of 06:51, 31 January 2018
Line 3:		Line 3:
	<StructureSection load='5df5' size='340' side='right' caption='[[5df5]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='5df5' size='340' side='right' caption='[[5df5]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c0z\|5c0z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c0z\|5c0z]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Cycs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [http://pdbe.org/5df5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [http://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [http://pdbe.org/5df5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [http://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]
	[[Category: Edwards, B F.P]]		[[Category: Edwards, B F.P]]

OCA at 15:23, 14 September 2016

OCA — Wed, 14 Sep 2016 15:23:27 GMT

←Older revision		Revision as of 15:23, 14 September 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5df5 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.==
		+	<StructureSection load='5df5' size='340' side='right' caption='[[5df5]], [[Resolution\|resolution]] 1.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5df5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DF5 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5c0z\|5c0z]]</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=5df5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df5 OCA], [http://pdbe.org/5df5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5df5 RCSB], [http://www.ebi.ac.uk/pdbsum/5df5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5df5 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CYC_RAT CYC_RAT]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Mammalian cytochrome c (Cytc) transfers electrons from the bc(1) complex to cytochrome c oxidase (CcO) as part of the mitochondrial electron transport chain, and it also participates in type II apoptosis. Our recent discovery of two tyrosine phosphorylation sites in Cytc, Tyr97 in bovine heart and Tyr48 in bovine liver, indicates that Cytc functions are regulated through cell signaling. To characterize the role of Cytc tyrosine phosphorylation in detail using an independent approach, we here overexpressed and purified a Tyr48Glu mutant Cytc, mimicking the in vivo Tyr48 phosphorylation found in cow liver, along with wild-type and Tyr48Phe variants as controls. The midpoint redox potential of the phosphomimetic mutant was decreased by 45 mV compared to control (192 vs 237 mV). Similar to Tyr48 in vivo phosphorylated Cytc, direct kinetic analysis of the Cytc reaction with isolated CcO revealed decreased V(max) for the Tyr48Glu mutant by 30% compared to wild type or the Tyr48Phe variants. Moreover, the phosphomimetic substitution resulted in major changes of Cytc functions related to apoptosis. The binding affinity of Tyr48Glu Cytc to cardiolipin was decreased by about 30% compared to wild type or the Tyr48Phe variants, and Cytc peroxidase activity of the Tyr48Glu mutant was cardiolipin-inducible only at high cardiolipin concentration, unlike controls. Importantly, the Tyr48Glu Cytc failed to induce any detectable downstream activation of caspase-3. Our data suggest that in vivo Tyr48 phosphorylation might serve as an antiapoptotic switch and highlight the strategic position and role of the conserved Cytc residue Tyr48 in regulating multiple functions of Cytc.

-	~~Authors~~:	+	Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation.,Pecina P, Borisenko GG, Belikova NA, Tyurina YY, Pecinova A, Lee I, Samhan-Arias AK, Przyklenk K, Kagan VE, Huttemann M Biochemistry. 2010 Aug 10;49(31):6705-14. doi: 10.1021/bi100486s. PMID:20586425<ref>PMID:20586425</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5df5" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Brunzelle, J S]]
		+	[[Category: Edwards, B F.P]]
		+	[[Category: Huttemann, M]]
		+	[[Category: Mahapatra, G]]
		+	[[Category: Vaishnav, A A]]
		+	[[Category: Cytochrome c]]
		+	[[Category: Electron transport]]
		+	[[Category: Mutant]]
		+	[[Category: Oxidized]]
		+	[[Category: Rat]]

OCA at 11:52, 15 May 2016

OCA — Sun, 15 May 2016 11:52:31 GMT

←Older revision		Revision as of 11:52, 15 May 2016
Line 3:		Line 3:
	The entry 5df5 is ON HOLD until Paper Publication		The entry 5df5 is ON HOLD until Paper Publication

-	Authors: ~~Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Edwards, B.F.P]]
-	[[Category: Brunzelle, J.S]]
-	[[Category: Vaishnav, A.A]]
-	[[Category: Mahapatra, G]]
-	[[Category: Huttemann, M]]

OCA at 11:07, 16 December 2015

OCA — Wed, 16 Dec 2015 11:07:12 GMT

←Older revision		Revision as of 11:07, 16 December 2015
Line 7:		Line 7:
	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
		+	[[Category: Edwards, B.F.P]]
		+	[[Category: Brunzelle, J.S]]
	[[Category: Vaishnav, A.A]]		[[Category: Vaishnav, A.A]]
	[[Category: Mahapatra, G]]		[[Category: Mahapatra, G]]
	[[Category: Huttemann, M]]		[[Category: Huttemann, M]]
-	[[Category: Edwards, B.F.P]]
-	[[Category: Brunzelle, J.S]]

OCA: Protected "5df5" [edit=sysop:move=sysop]

OCA — Wed, 02 Sep 2015 11:34:14 GMT

Protected "5df5" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:34, 2 September 2015

OCA: New page: '''Unreleased structure''' The entry 5df5 is ON HOLD until Paper Publication Authors: Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M. Description: [[Cat...

OCA — Wed, 02 Sep 2015 11:34:13 GMT

New page: '''Unreleased structure''' The entry 5df5 is ON HOLD until Paper Publication Authors: Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M. Description: [[Cat...

New page

'''Unreleased structure'''

The entry 5df5 is ON HOLD until Paper Publication

Authors: Edwards, B.F.P., Mahapatra, G., Vaishnav, A.A., Brunzelle, J.S., Huttemann, M.

Description:
[[Category: Unreleased Structures]]
[[Category: Vaishnav, A.A]]
[[Category: Mahapatra, G]]
[[Category: Huttemann, M]]
[[Category: Edwards, B.F.P]]
[[Category: Brunzelle, J.S]]