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Crystallization and preliminary crystallographic analysis of a chitinase from Clonostachys rosea
CrChi1 is a chitinase from the nematophagous fungus Clonostachys rosea that plays a role in the infection of nematodes. In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and...
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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2009-04, Vol.65 (4), p.386-388 |
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container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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creator | Gan, Zhongwei Yang, Jinkui Tao, Nan Lou, Zhiyong Mi, Qili Meng, Zhaohui Zhang, Ke-Qin |
description | CrChi1 is a chitinase from the nematophagous fungus Clonostachys rosea that plays a role in the infection of nematodes. In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and ammonium dihydrogen phosphate as precipitant and a 1.8 Å resolution X‐ray data set was collected from a single flash‐cooled crystal (100 K). The crystals belonged to space group P21, with unit‐cell parameters a = 44.1, b = 71.7, c = 59.1 Å, α = γ = 90, β = 91.3°. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.45 Å3 Da−1 and 40%, respectively. To our knowledge, this is the first structure determination study of a chitinase from a nematophagous fungus. |
doi_str_mv | 10.1107/S1744309109008379 |
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In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and ammonium dihydrogen phosphate as precipitant and a 1.8 Å resolution X‐ray data set was collected from a single flash‐cooled crystal (100 K). The crystals belonged to space group P21, with unit‐cell parameters a = 44.1, b = 71.7, c = 59.1 Å, α = γ = 90, β = 91.3°. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.45 Å3 Da−1 and 40%, respectively. 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Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>CrChi1 is a chitinase from the nematophagous fungus Clonostachys rosea that plays a role in the infection of nematodes. In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and ammonium dihydrogen phosphate as precipitant and a 1.8 Å resolution X‐ray data set was collected from a single flash‐cooled crystal (100 K). The crystals belonged to space group P21, with unit‐cell parameters a = 44.1, b = 71.7, c = 59.1 Å, α = γ = 90, β = 91.3°. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.45 Å3 Da−1 and 40%, respectively. To our knowledge, this is the first structure determination study of a chitinase from a nematophagous fungus.</description><subject>chitinases</subject><subject>Chitinases - chemistry</subject><subject>Clonostachys rosea</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>Hypocreales - enzymology</subject><subject>Nematoda</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhiMEoh_wA7ggn7il9UeSiS9IVUQXpFVRxZc4mYnjdA1OvLWzQPj1eLurtohDT7ZmnvfVOzNZ9oLRE8YonH5gUBSCSkYlpbUA-Sg73Jbybe3xvf9BdhTjd0qFkFX9NDtgUhQcajjMvjVhjhM6Z__gZP1IcOzIOhhnBztimIne9_1VwPXK6gSgm6ONxPcEiV7ZKYHRkD74gTTOjz7xejVHEnw0-Cx70qOL5vn-Pc4-nb_52LzNl-8X75qzZa4LEDIXCJqnqJgiQ90C0I61yABLLETZCd7pjtU9rzQUjEvRSi1b7GQrNAgOTBxnr3e-6007mE6bcQro1DrYIY2hPFr1b2e0K3XlfypeVQVUkAxe7Q2Cv96YOKnBRm2cw9H4TVQVMCaYLB4EOS2hoLJKINuBOm0iBtPfpmFUbQ-o_jtg0ry8P8adYn-xBMgd8Ms6Mz_sqM6-nvPlsmQ35vlOa-Nkft9qMfxI0wko1ZeLhfoMDW3qy4W6EH8B7aO38w</recordid><startdate>200904</startdate><enddate>200904</enddate><creator>Gan, Zhongwei</creator><creator>Yang, Jinkui</creator><creator>Tao, Nan</creator><creator>Lou, Zhiyong</creator><creator>Mi, Qili</creator><creator>Meng, Zhaohui</creator><creator>Zhang, Ke-Qin</creator><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200904</creationdate><title>Crystallization and preliminary crystallographic analysis of a chitinase from Clonostachys rosea</title><author>Gan, Zhongwei ; Yang, Jinkui ; Tao, Nan ; Lou, Zhiyong ; Mi, Qili ; Meng, Zhaohui ; Zhang, Ke-Qin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4739-3a7c2309a74478b770d1ba17a5a435d32dcd18f26c741293b9c9bad9b3c732713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>chitinases</topic><topic>Chitinases - chemistry</topic><topic>Clonostachys rosea</topic><topic>Crystallization</topic><topic>Crystallization Communications</topic><topic>Crystallography, X-Ray</topic><topic>Hypocreales - enzymology</topic><topic>Nematoda</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gan, Zhongwei</creatorcontrib><creatorcontrib>Yang, Jinkui</creatorcontrib><creatorcontrib>Tao, Nan</creatorcontrib><creatorcontrib>Lou, Zhiyong</creatorcontrib><creatorcontrib>Mi, Qili</creatorcontrib><creatorcontrib>Meng, Zhaohui</creatorcontrib><creatorcontrib>Zhang, Ke-Qin</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gan, Zhongwei</au><au>Yang, Jinkui</au><au>Tao, Nan</au><au>Lou, Zhiyong</au><au>Mi, Qili</au><au>Meng, Zhaohui</au><au>Zhang, Ke-Qin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary crystallographic analysis of a chitinase from Clonostachys rosea</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2009-04</date><risdate>2009</risdate><volume>65</volume><issue>4</issue><spage>386</spage><epage>388</epage><pages>386-388</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>CrChi1 is a chitinase from the nematophagous fungus Clonostachys rosea that plays a role in the infection of nematodes. In order to resolve the crystal structure of CrChi1 and to gain a better understanding of its biological functions, recombinant CrChi1 was crystallized at 291 K using PEG 3350 and ammonium dihydrogen phosphate as precipitant and a 1.8 Å resolution X‐ray data set was collected from a single flash‐cooled crystal (100 K). The crystals belonged to space group P21, with unit‐cell parameters a = 44.1, b = 71.7, c = 59.1 Å, α = γ = 90, β = 91.3°. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient and solvent content were calculated to be 2.45 Å3 Da−1 and 40%, respectively. To our knowledge, this is the first structure determination study of a chitinase from a nematophagous fungus.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>19342787</pmid><doi>10.1107/S1744309109008379</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | chitinases Chitinases - chemistry Clonostachys rosea Crystallization Crystallization Communications Crystallography, X-Ray Hypocreales - enzymology Nematoda |
title | Crystallization and preliminary crystallographic analysis of a chitinase from Clonostachys rosea |
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