MAD on threonine synthase: the phasing power of oxidized selenomethionine
The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure determination. In this paper, MAD data collected from oxidized and reduced selenomethionine‐containing protein are described, and it is shown that oxidi...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-09, Vol.57 (9), p.1337-1340 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Thomazeau, Karine Curien, Gilles Thompson, Andrew Dumas, Renaud Biou, Valérie |
| description | The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure determination. In this paper, MAD data collected from oxidized and reduced selenomethionine‐containing protein are described, and it is shown that oxidized selenomethionine has a very strong phasing power and can be efficiently used if the oxidation is uniform. The comparison was performed on threonine synthase crystals. For example, the phasing power of the oxidized data is doubled for the dispersive signal and is 20% stronger for the anomalous signal at the peak wavelength. The strength of the anomalous signal can be used to improve the signal when a protein contains few methionines or for single anomalous dispersion. The oxidation of some selenomethionines shows in the electron‐density map through the presence of water molecules within hydrogen‐bonding distance of the putative O atom. |
| doi_str_mv | 10.1107/S0907444901008666 |
| format | Article |
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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure determination. In this paper, MAD data collected from oxidized and reduced selenomethionine‐containing protein are described, and it is shown that oxidized selenomethionine has a very strong phasing power and can be efficiently used if the oxidation is uniform. The comparison was performed on threonine synthase crystals. For example, the phasing power of the oxidized data is doubled for the dispersive signal and is 20% stronger for the anomalous signal at the peak wavelength. The strength of the anomalous signal can be used to improve the signal when a protein contains few methionines or for single anomalous dispersion. The oxidation of some selenomethionines shows in the electron‐density map through the presence of water molecules within hydrogen‐bonding distance of the putative O atom.</description><subject>Arabidopsis - enzymology</subject><subject>Carbon-Oxygen Lyases - chemistry</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>MAD</subject><subject>Models, Molecular</subject><subject>Oxidation-Reduction</subject><subject>Protein Conformation</subject><subject>selenomethionine</subject><subject>Selenomethionine - chemistry</subject><subject>Spectrometry, Fluorescence</subject><subject>threonine synthase</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkLtOw0AQRVcIxPsDaJArOsPsw_ugixKeCqEAhKhWdjImC443eB1B-HoWEgESBdWMRudcjS4hexQOKQV1dAMGlBDCAAXQUsoVskm5MSmAUKu_9g2yFcITADDG1TrZoDRjknO9SS6uOr3E10k7btDXrsYkzOt2nAc8jjdMpnF19WMy9a_YJL5M_JsbuXccJQErrP0E27H7EnfIWplXAXeXc5vcnZ7cds_T_vXZRbfTT4dcC0hLw1jOGDVQ5JoJLuMvkBWaZ6IojBFZaWgBVPNRyQ0rpZC8NJpJVIYpGrltcrDInTb-ZYahtRMXhlhVeY1-FqyilBmhswjSBThsfAgNlnbauEnezC0F-9mf_dNfdPaX4bNigqMfY1lYBPQCeHUVzv9PtJ2H3uUA4jmq6UJ1ocW3bzVvnq1UXGX2fnBmrxTT3T4d2Fv-Ac0Qh84</recordid><startdate>200109</startdate><enddate>200109</enddate><creator>Thomazeau, Karine</creator><creator>Curien, Gilles</creator><creator>Thompson, Andrew</creator><creator>Dumas, Renaud</creator><creator>Biou, Valérie</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>200109</creationdate><title>MAD on threonine synthase: the phasing power of oxidized selenomethionine</title><author>Thomazeau, Karine ; Curien, Gilles ; Thompson, Andrew ; Dumas, Renaud ; Biou, Valérie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3840-f922a22190ba8243611505b8354bb9945f91b0183df392f6463f9826e79271b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Arabidopsis - enzymology</topic><topic>Carbon-Oxygen Lyases - chemistry</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>MAD</topic><topic>Models, Molecular</topic><topic>Oxidation-Reduction</topic><topic>Protein Conformation</topic><topic>selenomethionine</topic><topic>Selenomethionine - chemistry</topic><topic>Spectrometry, Fluorescence</topic><topic>threonine synthase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thomazeau, Karine</creatorcontrib><creatorcontrib>Curien, Gilles</creatorcontrib><creatorcontrib>Thompson, Andrew</creatorcontrib><creatorcontrib>Dumas, Renaud</creatorcontrib><creatorcontrib>Biou, Valérie</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>Thomazeau, Karine</au><au>Curien, Gilles</au><au>Thompson, Andrew</au><au>Dumas, Renaud</au><au>Biou, Valérie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MAD on threonine synthase: the phasing power of oxidized selenomethionine</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2001-09</date><risdate>2001</risdate><volume>57</volume><issue>9</issue><spage>1337</spage><epage>1340</epage><pages>1337-1340</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure determination. In this paper, MAD data collected from oxidized and reduced selenomethionine‐containing protein are described, and it is shown that oxidized selenomethionine has a very strong phasing power and can be efficiently used if the oxidation is uniform. The comparison was performed on threonine synthase crystals. For example, the phasing power of the oxidized data is doubled for the dispersive signal and is 20% stronger for the anomalous signal at the peak wavelength. The strength of the anomalous signal can be used to improve the signal when a protein contains few methionines or for single anomalous dispersion. The oxidation of some selenomethionines shows in the electron‐density map through the presence of water molecules within hydrogen‐bonding distance of the putative O atom.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>11526338</pmid><doi>10.1107/S0907444901008666</doi><tpages>4</tpages></addata></record> |
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| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE; Crystallography Journals Online; Alma/SFX Local Collection |
| subjects | Arabidopsis - enzymology Carbon-Oxygen Lyases - chemistry Crystallization Crystallography, X-Ray MAD Models, Molecular Oxidation-Reduction Protein Conformation selenomethionine Selenomethionine - chemistry Spectrometry, Fluorescence threonine synthase |
| title | MAD on threonine synthase: the phasing power of oxidized selenomethionine |
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