Oxygen-bound hell's gate globin I by classical versus LB nanotemplate method
X‐ray atomic structure of recombinant Hell's gate globin I (HGbI) from Methylacidophilum infernorum was calculated from the X‐ray diffraction data of two different types of crystals: obtained by classical hanging drop and by LB nanotemplate method under the same crystallization conditions. Afte...
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Veröffentlicht in: | Journal of cellular biochemistry 2012-07, Vol.113 (7), p.2543-2548 |
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description | X‐ray atomic structure of recombinant Hell's gate globin I (HGbI) from Methylacidophilum infernorum was calculated from the X‐ray diffraction data of two different types of crystals: obtained by classical hanging drop and by LB nanotemplate method under the same crystallization conditions. After the accurate comparison of crystallographic parameters and electron density maps of two structures they appears to be quite similar, while the quality of the crystals grown by LB nanotemplate method was higher then of those grown by classical method. Indeed, the resolution of the LB crystal structure was 1.65 Å, while classical crystals showed only 3.2 Å resolution. Moreover, the reproducibility of this result in the case of LB crystals was much better—nine crystals from 10 gave the same structural results, while only two of 10 classical crystals were appropriate for the X‐ray structure resolution. J. Cell. Biochem. 113: 2543–2548, 2012. © 2012 Wiley Periodicals, Inc. |
doi_str_mv | 10.1002/jcb.24131 |
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After the accurate comparison of crystallographic parameters and electron density maps of two structures they appears to be quite similar, while the quality of the crystals grown by LB nanotemplate method was higher then of those grown by classical method. Indeed, the resolution of the LB crystal structure was 1.65 Å, while classical crystals showed only 3.2 Å resolution. Moreover, the reproducibility of this result in the case of LB crystals was much better—nine crystals from 10 gave the same structural results, while only two of 10 classical crystals were appropriate for the X‐ray structure resolution. J. Cell. 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Cell. Biochem</addtitle><description>X‐ray atomic structure of recombinant Hell's gate globin I (HGbI) from Methylacidophilum infernorum was calculated from the X‐ray diffraction data of two different types of crystals: obtained by classical hanging drop and by LB nanotemplate method under the same crystallization conditions. After the accurate comparison of crystallographic parameters and electron density maps of two structures they appears to be quite similar, while the quality of the crystals grown by LB nanotemplate method was higher then of those grown by classical method. Indeed, the resolution of the LB crystal structure was 1.65 Å, while classical crystals showed only 3.2 Å resolution. Moreover, the reproducibility of this result in the case of LB crystals was much better—nine crystals from 10 gave the same structural results, while only two of 10 classical crystals were appropriate for the X‐ray structure resolution. J. Cell. Biochem. 113: 2543–2548, 2012. © 2012 Wiley Periodicals, Inc.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Globins - chemistry</subject><subject>Globins - metabolism</subject><subject>HELL'S GATE GLOBIN I</subject><subject>Hemoglobins</subject><subject>LANGMUIR BLODGETT</subject><subject>Oxygen - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>THIN FILM</subject><subject>Verrucomicrobia - chemistry</subject><subject>Verrucomicrobia - metabolism</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10EtPwkAUBeCJ0QiiC_-AmZ26KM6jz6UQeZhGYoLobjKdBxT7wE6r9N9bLLBzdTffObk5AFxj1McIkYe1iPrExhSfgC5GgWfZrm2fgi7yKLIIxaQDLoxZI4SCgJJz0CGNdgKKuiCcbeulyqworzIJVypJbg1c8lLBZZJHcQanMKqhSLgxseAJ_FaFqQwMBzDjWV6qdJPscKrKVS4vwZnmiVFX-9sDb6On-XBihbPxdPgYWoK6FFuaECm1xyMppA5siaNABxz5DsY-dqgWWhLqKqx9JBzp-8jGkjiEEu473EYR7YG7tndT5F-VMiVLYyOa33mm8sowjDDxbJ-6pKH3LRVFbkyhNNsUccqLukFsNx5rxmN_4zX2Zl9bRamSR3lYqwEPLfiJE1X_38Seh4NDpdUmYlOq7THBi0_metRz2PvLmL0uPhYjH03YnP4CUdSG3w</recordid><startdate>201207</startdate><enddate>201207</enddate><creator>Pechkova, Eugenia</creator><creator>Scudieri, Dora</creator><creator>Belmonte, Luca</creator><creator>Nicolini, Claudio</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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>201207</creationdate><title>Oxygen-bound hell's gate globin I by classical versus LB nanotemplate method</title><author>Pechkova, Eugenia ; Scudieri, Dora ; Belmonte, Luca ; Nicolini, Claudio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3631-f22ddf7abdcdf94d1b9f9a085118153fcfd236e1f80c5d88041d25232a85a40b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Globins - chemistry</topic><topic>Globins - metabolism</topic><topic>HELL'S GATE GLOBIN I</topic><topic>Hemoglobins</topic><topic>LANGMUIR BLODGETT</topic><topic>Oxygen - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>THIN FILM</topic><topic>Verrucomicrobia - chemistry</topic><topic>Verrucomicrobia - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pechkova, Eugenia</creatorcontrib><creatorcontrib>Scudieri, Dora</creatorcontrib><creatorcontrib>Belmonte, Luca</creatorcontrib><creatorcontrib>Nicolini, Claudio</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>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pechkova, Eugenia</au><au>Scudieri, Dora</au><au>Belmonte, Luca</au><au>Nicolini, Claudio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxygen-bound hell's gate globin I by classical versus LB nanotemplate method</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J. Cell. Biochem</addtitle><date>2012-07</date><risdate>2012</risdate><volume>113</volume><issue>7</issue><spage>2543</spage><epage>2548</epage><pages>2543-2548</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><abstract>X‐ray atomic structure of recombinant Hell's gate globin I (HGbI) from Methylacidophilum infernorum was calculated from the X‐ray diffraction data of two different types of crystals: obtained by classical hanging drop and by LB nanotemplate method under the same crystallization conditions. After the accurate comparison of crystallographic parameters and electron density maps of two structures they appears to be quite similar, while the quality of the crystals grown by LB nanotemplate method was higher then of those grown by classical method. Indeed, the resolution of the LB crystal structure was 1.65 Å, while classical crystals showed only 3.2 Å resolution. Moreover, the reproducibility of this result in the case of LB crystals was much better—nine crystals from 10 gave the same structural results, while only two of 10 classical crystals were appropriate for the X‐ray structure resolution. J. Cell. Biochem. 113: 2543–2548, 2012. © 2012 Wiley Periodicals, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>22415930</pmid><doi>10.1002/jcb.24131</doi><tpages>6</tpages></addata></record> |
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subjects | Bacterial Proteins - chemistry Bacterial Proteins - metabolism Crystallization Crystallography, X-Ray Globins - chemistry Globins - metabolism HELL'S GATE GLOBIN I Hemoglobins LANGMUIR BLODGETT Oxygen - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism THIN FILM Verrucomicrobia - chemistry Verrucomicrobia - metabolism |
title | Oxygen-bound hell's gate globin I by classical versus LB nanotemplate method |
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