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Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana

The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% (Rfree = 18.4%) at 1.60 Å resolution. The refined struc...

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Published in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-07, Vol.61 (7), p.647-650
Main Authors:	Allard, Simon T. M., Bingman, Craig A., Johnson, Kenneth A., Bitto, Eduard, Jeon, Won Bae, Wesenberg, Gary E., Phillips Jr, George N.
Format:	Article
Language:	English
Subjects:	Arabidopsis - metabolism Arabidopsis thaliana At3g22680 Cholic Acids - pharmacology Cloning, Molecular Crystallization Crystallography, X-Ray - methods Detergents - pharmacology Electrophoresis, Polyacrylamide Gel Models, Statistical Protein Conformation Selenomethionine - chemistry Streptomyces coelicolor - metabolism Structural Genomics Communications X-Ray Diffraction
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cited_by	cdi_FETCH-LOGICAL-c3843-5be1c12d6460a5573c15b0a203be30820e1dc2743dd69a38c04c287f59f831ea3
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container_issue	7
container_start_page	647
container_title	Acta crystallographica. Section F, Structural biology and crystallization communications
container_volume	61
creator	Allard, Simon T. M. Bingman, Craig A. Johnson, Kenneth A. Bitto, Eduard Jeon, Won Bae Wesenberg, Gary E. Phillips Jr, George N.
description	The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% (Rfree = 18.4%) at 1.60 Å resolution. The refined structure shows one monomer in the asymmetric unit, with one molecule of the non‐denaturing detergent CHAPS {3‐[(3‐cholamidopropyl)dimethylammonio]‐1‐propane sulfonate} tightly bound. Protein At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformation space.
doi_str_mv	10.1107/S1744309105019743
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M. ; Bingman, Craig A. ; Johnson, Kenneth A. ; Bitto, Eduard ; Jeon, Won Bae ; Wesenberg, Gary E. ; Phillips Jr, George N.</creator><creatorcontrib>Allard, Simon T. M. ; Bingman, Craig A. ; Johnson, Kenneth A. ; Bitto, Eduard ; Jeon, Won Bae ; Wesenberg, Gary E. ; Phillips Jr, George N. ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% (Rfree = 18.4%) at 1.60 Å resolution. The refined structure shows one monomer in the asymmetric unit, with one molecule of the non‐denaturing detergent CHAPS {3‐[(3‐cholamidopropyl)dimethylammonio]‐1‐propane sulfonate} tightly bound. Protein At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformation space.</description><identifier>ISSN: 1744-3091</identifier><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309105019743</identifier><identifier>PMID: 16511118</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Arabidopsis - metabolism ; Arabidopsis thaliana ; At3g22680 ; Cholic Acids - pharmacology ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray - methods ; Detergents - pharmacology ; Electrophoresis, Polyacrylamide Gel ; Models, Statistical ; Protein Conformation ; Selenomethionine - chemistry ; Streptomyces coelicolor - metabolism ; Structural Genomics Communications ; X-Ray Diffraction</subject><ispartof>Acta crystallographica. 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M.</creatorcontrib><creatorcontrib>Bingman, Craig A.</creatorcontrib><creatorcontrib>Johnson, Kenneth A.</creatorcontrib><creatorcontrib>Bitto, Eduard</creatorcontrib><creatorcontrib>Jeon, Won Bae</creatorcontrib><creatorcontrib>Wesenberg, Gary E.</creatorcontrib><creatorcontrib>Phillips Jr, George N.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% (Rfree = 18.4%) at 1.60 Å resolution. The refined structure shows one monomer in the asymmetric unit, with one molecule of the non‐denaturing detergent CHAPS {3‐[(3‐cholamidopropyl)dimethylammonio]‐1‐propane sulfonate} tightly bound. Protein At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformation space.</description><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>At3g22680</subject><subject>Cholic Acids - pharmacology</subject><subject>Cloning, Molecular</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray - methods</subject><subject>Detergents - pharmacology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Models, Statistical</subject><subject>Protein Conformation</subject><subject>Selenomethionine - chemistry</subject><subject>Streptomyces coelicolor - metabolism</subject><subject>Structural Genomics Communications</subject><subject>X-Ray Diffraction</subject><issn>1744-3091</issn><issn>2053-230X</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkc1u1DAUhS1ERduBB2CDLBbsUvwTx84GaVQxBVG1ixlArCzHuZkxZOKp7UC7Y9Mn4014EhJl1BaxwBtb937nXF8dhJ5TckIpka-XVOY5JyUlgtBS5vwROhpL2Vh7_OB9iI5j_EoI52WhnqBDWgg6HHWE7DKF3qY-ADYJ05Pi98_bX7c4QPRtn5zvsG9w2gDeBZ_AdbgJfovX0AFuve0jnie-ZqxQZOrMg6lc7XfRxUFmWmc68xQdNKaN8Gx_z9DHxdvV6bvs_PLs_en8PLNc5TwTFVBLWV3kBTFCSG6pqIhhhFfAiWIEaG3ZsGVdF6XhypLcMiUbUTaKUzB8ht5Mvru-2kJtoUvBtHoX3NaEG-2N0393OrfRa_9d01KwXJLB4OVk4GNyOlqXwG6s7zqwSVPGeMlH6NV-SvBXPcSkty5aaFvTge-jloTmUik1gHQCbfAxBmjufkKJHvPT_-Q3aF48XOFesQ9sAMoJ-OFauPm_o55_WbDVSozZz1A2aV1McH2nNeGbLiSXQn--ONN8yT4syk-FJvwPix21Qw</recordid><startdate>200507</startdate><enddate>200507</enddate><creator>Allard, Simon T. 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M. ; Bingman, Craig A. ; Johnson, Kenneth A. ; Bitto, Eduard ; Jeon, Won Bae ; Wesenberg, Gary E. ; Phillips Jr, George N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3843-5be1c12d6460a5573c15b0a203be30820e1dc2743dd69a38c04c287f59f831ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>At3g22680</topic><topic>Cholic Acids - pharmacology</topic><topic>Cloning, Molecular</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray - methods</topic><topic>Detergents - pharmacology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Models, Statistical</topic><topic>Protein Conformation</topic><topic>Selenomethionine - chemistry</topic><topic>Streptomyces coelicolor - metabolism</topic><topic>Structural Genomics Communications</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Allard, Simon T. M.</creatorcontrib><creatorcontrib>Bingman, Craig A.</creatorcontrib><creatorcontrib>Johnson, Kenneth A.</creatorcontrib><creatorcontrib>Bitto, Eduard</creatorcontrib><creatorcontrib>Jeon, Won Bae</creatorcontrib><creatorcontrib>Wesenberg, Gary E.</creatorcontrib><creatorcontrib>Phillips Jr, George N.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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F</addtitle><date>2005-07</date><risdate>2005</risdate><volume>61</volume><issue>7</issue><spage>647</spage><epage>650</epage><pages>647-650</pages><issn>1744-3091</issn><issn>2053-230X</issn><eissn>1744-3091</eissn><eissn>2053-230X</eissn><abstract>The gene product of At3g22680 from Arabidopsis thaliana codes for a protein of unknown function. The crystal structure of the At3g22680 gene product was determined by multiple‐wavelength anomalous diffraction and refined to an R factor of 16.0% (Rfree = 18.4%) at 1.60 Å resolution. The refined structure shows one monomer in the asymmetric unit, with one molecule of the non‐denaturing detergent CHAPS {3‐[(3‐cholamidopropyl)dimethylammonio]‐1‐propane sulfonate} tightly bound. Protein At3g22680 shows no structural homology to any other known proteins and represents a new fold in protein conformation space.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>16511118</pmid><doi>10.1107/S1744309105019743</doi><tpages>4</tpages></addata></record>
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source	Open Access: PubMed Central; Wiley-Blackwell Read & Publish Collection
subjects	Arabidopsis - metabolism Arabidopsis thaliana At3g22680 Cholic Acids - pharmacology Cloning, Molecular Crystallization Crystallography, X-Ray - methods Detergents - pharmacology Electrophoresis, Polyacrylamide Gel Models, Statistical Protein Conformation Selenomethionine - chemistry Streptomyces coelicolor - metabolism Structural Genomics Communications X-Ray Diffraction
title	Structure at 1.6 Å resolution of the protein from gene locus At3g22680 from Arabidopsis thaliana
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