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Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli
The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. Crystals grew as orthorhombic plates with cell dimensions a = 58 A, b = 73 A, and c = 205 A. The asymmetric unit probably contains one B2 dimer of molecular weight 2 X 43...
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Published in: | The Journal of biological chemistry 1984-07, Vol.259 (14), p.9076-9077 |
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container_end_page | 9077 |
container_issue | 14 |
container_start_page | 9076 |
container_title | The Journal of biological chemistry |
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creator | Joelson, T Uhlin, U Eklund, H Sjöberg, B M Hahne, S Karlsson, M |
description | The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. Crystals grew as orthorhombic plates with cell dimensions a = 58 A, b = 73 A, and c = 205 A. The asymmetric unit probably contains one B2 dimer of molecular weight 2 X 43,000. The packing of molecules in the crystals is compatible with an elongated shape of the dimer. The crystals diffract to 2.5 A and are suitable for structural work. |
doi_str_mv | 10.1016/S0021-9258(17)47266-8 |
format | article |
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Psychology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Macromolecular Substances</topic><topic>Oxidoreductases</topic><topic>Protein Conformation</topic><topic>Ribonucleotide Reductases - isolation & purification</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joelson, T</creatorcontrib><creatorcontrib>Uhlin, U</creatorcontrib><creatorcontrib>Eklund, H</creatorcontrib><creatorcontrib>Sjöberg, B M</creatorcontrib><creatorcontrib>Hahne, S</creatorcontrib><creatorcontrib>Karlsson, M</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joelson, T</au><au>Uhlin, U</au><au>Eklund, H</au><au>Sjöberg, B M</au><au>Hahne, S</au><au>Karlsson, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1984-07-25</date><risdate>1984</risdate><volume>259</volume><issue>14</issue><spage>9076</spage><epage>9077</epage><pages>9076-9077</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. 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subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrogen-Ion Concentration Macromolecular Substances Oxidoreductases Protein Conformation Ribonucleotide Reductases - isolation & purification X-Ray Diffraction |
title | Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli |
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