4qrm - Revision history

OCA at 12:48, 1 March 2024

OCA — Fri, 01 Mar 2024 12:48:19 GMT

←Older revision		Revision as of 12:48, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRM 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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [https://pdbe.org/4qrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [https://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm 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]] 4.315Å</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [https://pdbe.org/4qrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [https://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).		[https://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	At the base of the bacterial flagella, a cytoplasmic rotor (the C-ring) generates torque and reverses rotation sense in response to stimuli. The bulk of the C-ring forms from many copies of the proteins FliG, FliM, and FliN, which together constitute the switch complex. To help resolve outstanding issues regarding C-ring architecture, we have investigated interactions between FliM and FliG from Thermotoga maritima with X-ray crystallography and pulsed dipolar ESR spectroscopy (PDS). A new crystal structure of an 11-unit FliG:FliM complex produces a large arc with a curvature consistent with the dimensions of the C-ring. Previously determined structures along with this new structure provided a basis to test switch complex assembly models. PDS combined with mutational studies and targeted cross-linking reveal that FliM and FliG interact through their middle domains to form both parallel and antiparallel arrangements in solution. Residue substitutions at predicted interfaces disrupt higher-order complexes that are primarily mediated by contacts between the C-terminal domain of FliG and the middle domain of a neighboring FliG molecule. Spin separations among multi-labeled components fit a self-consistent model that agree well with electron microscopy images of the C-ring. An activated form of the response regulator CheY destabilizes the parallel arrangement of FliM molecules to perturb FliG alignment in a process that may reflect the onset of rotation switching. These data suggest a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly and cooperative transitions.
-
-	Assembly states of FliM and FliG within the flagellar switch complex.,Sircar R, Borbat PP, Lynch MJ, Bhatnagar J, Beyersdorf MS, Halkides CJ, Freed JH, Crane BR J Mol Biol. 2015 Feb 27;427(4):867-86. doi: 10.1016/j.jmb.2014.12.009. Epub 2014 , Dec 20. PMID:25536293<ref>PMID:25536293</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4qrm" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]		*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 13:48, 22 February 2023

OCA — Wed, 22 Feb 2023 13:48:59 GMT

←Older revision		Revision as of 13:48, 22 February 2023
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	<StructureSection load='4qrm' size='340' side='right'caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>		<StructureSection load='4qrm' size='340' side='right'caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Thema Thema~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4QRM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QRM FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fliM, TM_0679, ThemaDRAFT_0623 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), fliG, TM_0220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [https://pdbe.org/4qrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [https://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm 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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [~~http~~://pdbe.org/4qrm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA]] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). [[http://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).	+	[https://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4qrm" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4qrm" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Flagellar protein 3D structures\|Flagellar protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Thema~~]]	+	[[Category: Thermotoga maritima MSB8]]
-	[[Category: Crane~~, B R~~]]	+	[[Category: Crane BR]]
-	[[Category: Sircar, R]]	+	[[Category: Sircar R]]
-	~~[[Category: Flagellar rotor protein]]~~	+
-	~~[[Category: Protein binding~~]]	+

OCA at 09:08, 24 April 2019

OCA — Wed, 24 Apr 2019 09:08:22 GMT

←Older revision		Revision as of 09:08, 24 April 2019
Line 1:		Line 1:

	==crystal structure of a binary complex of FliM-FliG middle domains from T.maritima==		==crystal structure of a binary complex of FliM-FliG middle domains from T.maritima==
-	<StructureSection load='4qrm' size='340' side='right' caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>	+	<StructureSection load='4qrm' size='340' side='right'caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRM FirstGlance]. <br>
-	</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [http://pdbe.org/4qrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [http://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fliM, TM_0679, ThemaDRAFT_0623 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA]), fliG, TM_0220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [http://pdbe.org/4qrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [http://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Thema]]
	[[Category: Crane, B R]]		[[Category: Crane, B R]]
	[[Category: Sircar, R]]		[[Category: Sircar, R]]
	[[Category: Flagellar rotor protein]]		[[Category: Flagellar rotor protein]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 02:08, 11 March 2017

OCA — Sat, 11 Mar 2017 02:08:13 GMT

←Older revision		Revision as of 02:08, 11 March 2017
Line 1:		Line 1:
		+
	==crystal structure of a binary complex of FliM-FliG middle domains from T.maritima==		==crystal structure of a binary complex of FliM-FliG middle domains from T.maritima==
	<StructureSection load='4qrm' size='340' side='right' caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>		<StructureSection load='4qrm' size='340' side='right' caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRM FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRM FirstGlance]. <br>
-	</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [http://www.ebi.ac.uk/pdbsum/4qrm PDBsum]</span></td></tr>	+	</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [http://pdbe.org/4qrm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [http://www.ebi.ac.uk/pdbsum/4qrm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qrm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4qrm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:02, 10 June 2015

OCA — Wed, 10 Jun 2015 14:02:22 GMT

←Older revision		Revision as of 14:02, 10 June 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==crystal structure of a binary complex of FliM-FliG middle domains from T.maritima==
		+	<StructureSection load='4qrm' size='340' side='right' caption='[[4qrm]], [[Resolution\|resolution]] 4.32Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4qrm]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QRM FirstGlance]. <br>
		+	</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=4qrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qrm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qrm RCSB], [http://www.ebi.ac.uk/pdbsum/4qrm PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FLIM_THEMA FLIM_THEMA]] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). [[http://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	At the base of the bacterial flagella, a cytoplasmic rotor (the C-ring) generates torque and reverses rotation sense in response to stimuli. The bulk of the C-ring forms from many copies of the proteins FliG, FliM, and FliN, which together constitute the switch complex. To help resolve outstanding issues regarding C-ring architecture, we have investigated interactions between FliM and FliG from Thermotoga maritima with X-ray crystallography and pulsed dipolar ESR spectroscopy (PDS). A new crystal structure of an 11-unit FliG:FliM complex produces a large arc with a curvature consistent with the dimensions of the C-ring. Previously determined structures along with this new structure provided a basis to test switch complex assembly models. PDS combined with mutational studies and targeted cross-linking reveal that FliM and FliG interact through their middle domains to form both parallel and antiparallel arrangements in solution. Residue substitutions at predicted interfaces disrupt higher-order complexes that are primarily mediated by contacts between the C-terminal domain of FliG and the middle domain of a neighboring FliG molecule. Spin separations among multi-labeled components fit a self-consistent model that agree well with electron microscopy images of the C-ring. An activated form of the response regulator CheY destabilizes the parallel arrangement of FliM molecules to perturb FliG alignment in a process that may reflect the onset of rotation switching. These data suggest a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly and cooperative transitions.

-	~~The entry 4qrm is ON HOLD until Paper Publication~~	+	Assembly states of FliM and FliG within the flagellar switch complex.,Sircar R, Borbat PP, Lynch MJ, Bhatnagar J, Beyersdorf MS, Halkides CJ, Freed JH, Crane BR J Mol Biol. 2015 Feb 27;427(4):867-86. doi: 10.1016/j.jmb.2014.12.009. Epub 2014 , Dec 20. PMID:25536293<ref>PMID:25536293</ref>

-	~~Authors: Crane~~, B.R.~~, Sircar, R~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
-	[[Category: Crane, B.R]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Crane, B R]]
	[[Category: Sircar, R]]		[[Category: Sircar, R]]
		+	[[Category: Flagellar rotor protein]]
		+	[[Category: Protein binding]]

OCA at 16:04, 24 December 2014

OCA — Wed, 24 Dec 2014 16:04:40 GMT

←Older revision		Revision as of 16:04, 24 December 2014
Line 6:		Line 6:

	Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima		Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima
		+	[[Category: Unreleased Structures]]
		+	[[Category: Crane, B.R]]
		+	[[Category: Sircar, R]]

OCA at 06:51, 27 August 2014

OCA — Wed, 27 Aug 2014 06:51:40 GMT

←Older revision		Revision as of 06:51, 27 August 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4qrm is ON HOLD	+	The entry 4qrm is ON HOLD until Paper Publication

	Authors: Crane, B.R., Sircar, R.		Authors: Crane, B.R., Sircar, R.

	Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima		Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima

OCA at 07:12, 23 July 2014

OCA — Wed, 23 Jul 2014 07:12:15 GMT

←Older revision		Revision as of 07:12, 23 July 2014
Line 3:		Line 3:
	The entry 4qrm is ON HOLD		The entry 4qrm is ON HOLD

-	Authors: Crane, B. R., Sircar, R	+	Authors: Crane, B.R., Sircar, R.

	Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima		Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima

OCA: Protected "4qrm" [edit=sysop:move=sysop]

OCA — Wed, 09 Jul 2014 06:53:20 GMT

Protected "4qrm" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:53, 9 July 2014

OCA: New page: '''Unreleased structure''' The entry 4qrm is ON HOLD Authors: Crane, B. R., Sircar, R Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima

OCA — Wed, 09 Jul 2014 06:53:19 GMT

New page: '''Unreleased structure''' The entry 4qrm is ON HOLD Authors: Crane, B. R., Sircar, R Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima

New page

'''Unreleased structure'''

The entry 4qrm is ON HOLD

Authors: Crane, B. R., Sircar, R

Description: crystal structure of a binary complex of FliM-FliG middle domains from T.maritima