Crystallization and preliminary X-ray diffraction studies of a novel alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
A novel alcohol dehydrogenase enzyme has been cloned from the hyperthermophilic archaeon Aeropyrum pernix and overexpressed in Escherichia coli. This zinc‐containing enzyme has been crystallized by the sitting‐drop vapour‐diffusion method using PEG 600 as precipitant. The crystals diffract to 1.5 Å...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-01, Vol.59 (1), p.174-176 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Guy, Jodie E. Isupov, Michail N. Littlechild, Jennifer A. |
| description | A novel alcohol dehydrogenase enzyme has been cloned from the hyperthermophilic archaeon Aeropyrum pernix and overexpressed in Escherichia coli. This zinc‐containing enzyme has been crystallized by the sitting‐drop vapour‐diffusion method using PEG 600 as precipitant. The crystals diffract to 1.5 Å resolution and belong to the orthorhombic space group P21212, with unit‐cell parameters a = 100.7, b = 103.2, c = 67.5 Å. The asymmetric unit contains two enzyme monomers. Two synchrotron data sets have been collected: one at a wavelength near the absorption edge of zinc and one at a remote wavelength. Three strong zinc‐ion positions were visible in the anomalous Patterson map. Two additional weaker zinc ions have been identified by anomalous Fourier synthesis. |
| doi_str_mv | 10.1107/S0907444902019649 |
| format | Article |
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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>A novel alcohol dehydrogenase enzyme has been cloned from the hyperthermophilic archaeon Aeropyrum pernix and overexpressed in Escherichia coli. This zinc‐containing enzyme has been crystallized by the sitting‐drop vapour‐diffusion method using PEG 600 as precipitant. The crystals diffract to 1.5 Å resolution and belong to the orthorhombic space group P21212, with unit‐cell parameters a = 100.7, b = 103.2, c = 67.5 Å. The asymmetric unit contains two enzyme monomers. Two synchrotron data sets have been collected: one at a wavelength near the absorption edge of zinc and one at a remote wavelength. Three strong zinc‐ion positions were visible in the anomalous Patterson map. Two additional weaker zinc ions have been identified by anomalous Fourier synthesis.</description><subject>Aeropyrum pernix</subject><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Alcohol Dehydrogenase - genetics</subject><subject>Alcohol Dehydrogenase - metabolism</subject><subject>alcohol dehydrogenases</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Cloning, Molecular</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Desulfurococcaceae - enzymology</subject><subject>Fourier Analysis</subject><subject>oxidoreductases</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Synchrotrons</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1TAQRSMEoqXwAWyQV-xS7EleHC-fArRIVRECBO3Gcu0xMThxaifQ8BP8Mi7vCZBYsPLIOudKc6coHjN6zBjlz95SQXld14ICZaKpxZ3ikFVClJTW_O5f80HxIKXPlFKAit8vDhjUQmwaOCx-dHFNs_LefVezCyNRoyFTRO8GN6q4ko9lVCsxztqo9C8izYtxmEiwRJExfEVPlNehD54Y7FcTwyccVUJiYxjI3CPp1wljHuIQpt55p4mKuleYw7YYw7TGZSAZGd3Nw-KeVT7ho_17VLx_-eJdd1qevT551W3PSl21NZQN1w0IBItVazgoIyxeWQ1glNGADQOV14b8rU1uB1ktuGAMULTAeQ3VUfF0lzvFcL1gmuXgkkbv1YhhSZJDKzgwkUG2A3UMKUW0copuyM1IRuXtFeQ_V8jOk334cjWg-WPsa89AuwO-OY_r_xPl9uJ5d0Fpe6uWO9WlGW9-qyp-kQ2v-EZ-OD-Rl5vLrn1DqTyvfgKpAqVi</recordid><startdate>200301</startdate><enddate>200301</enddate><creator>Guy, Jodie E.</creator><creator>Isupov, Michail N.</creator><creator>Littlechild, Jennifer A.</creator><general>Munksgaard International Publishers</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>7X8</scope></search><sort><creationdate>200301</creationdate><title>Crystallization and preliminary X-ray diffraction studies of a novel alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix</title><author>Guy, Jodie E. ; Isupov, Michail N. ; Littlechild, Jennifer A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3842-67c629e2fe38d72ad9febfc22dadc2e612a0472d9fcd902e14979112e98277423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aeropyrum pernix</topic><topic>Alcohol Dehydrogenase - chemistry</topic><topic>Alcohol Dehydrogenase - genetics</topic><topic>Alcohol Dehydrogenase - metabolism</topic><topic>alcohol dehydrogenases</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Cloning, Molecular</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Desulfurococcaceae - enzymology</topic><topic>Fourier Analysis</topic><topic>oxidoreductases</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Synchrotrons</topic><topic>Zinc - chemistry</topic><topic>Zinc - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guy, Jodie E.</creatorcontrib><creatorcontrib>Isupov, Michail N.</creatorcontrib><creatorcontrib>Littlechild, Jennifer A.</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><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guy, Jodie E.</au><au>Isupov, Michail N.</au><au>Littlechild, Jennifer A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray diffraction studies of a novel alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2003-01</date><risdate>2003</risdate><volume>59</volume><issue>1</issue><spage>174</spage><epage>176</epage><pages>174-176</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>A novel alcohol dehydrogenase enzyme has been cloned from the hyperthermophilic archaeon Aeropyrum pernix and overexpressed in Escherichia coli. This zinc‐containing enzyme has been crystallized by the sitting‐drop vapour‐diffusion method using PEG 600 as precipitant. The crystals diffract to 1.5 Å resolution and belong to the orthorhombic space group P21212, with unit‐cell parameters a = 100.7, b = 103.2, c = 67.5 Å. The asymmetric unit contains two enzyme monomers. Two synchrotron data sets have been collected: one at a wavelength near the absorption edge of zinc and one at a remote wavelength. Three strong zinc‐ion positions were visible in the anomalous Patterson map. Two additional weaker zinc ions have been identified by anomalous Fourier synthesis.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>12499562</pmid><doi>10.1107/S0907444902019649</doi><tpages>3</tpages></addata></record> |
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| identifier | ISSN: 1399-0047 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2003-01, Vol.59 (1), p.174-176 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Aeropyrum pernix Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism alcohol dehydrogenases Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Cloning, Molecular Crystallization Crystallography, X-Ray Desulfurococcaceae - enzymology Fourier Analysis oxidoreductases Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Synchrotrons Zinc - chemistry Zinc - metabolism |
| title | Crystallization and preliminary X-ray diffraction studies of a novel alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix |
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