{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:09:59Z","timestamp":1791274199099,"version":"4.1.0"},"reference-count":27,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,2,3]],"date-time":"2004-02-03T00:00:00Z","timestamp":1075766400000},"content-version":"vor","delay-in-days":3595,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[1994,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We have initiated a project to determine the three\u2010dimensional structure of GMP synthetase (GMPS) from <jats:italic>Escherichia coli<\/jats:italic>. GMPS catalyzes the conversion of XMP to GMP in the final step of de novo guanine nucleotide biosynthesis, and is a member of the glutamine amidotransferase family: a group of enzymes responsible for the assimilation of nitrogen into compounds such as amino acids, purine and pyrimidine bases, amino sugars, and antibiotics. The <jats:italic>E. coli guaA<\/jats:italic> gene encoding GMPS was cloned into a <jats:italic>tac<\/jats:italic> expression vector, overexpressed, and its gene product purified. Conditions for the growth of protein crystals were developed using recombinant GMPS in the presence of MgCl<jats:sub>2<\/jats:sub>, ATP, and XMP. The crystals are monoclinic, space group <jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>, with cell parameters of <jats:italic>a<\/jats:italic> = 156.0 \u00c5, <jats:italic>b<\/jats:italic> = 102.0 \u00c5, <jats:italic>c<\/jats:italic> = 78.8 \u00c5, \u03b2= 96.7\u00b0. Diffraction data to 2.8 \u00c5 spacings were collected on a Xuong\u2010Hamlin area detector with an overall <jats:italic>R<\/jats:italic><jats:sub>sym<\/jats:sub> of 5.2%. Both the volume of the unit cell and the peaks in the self\u2010rotation function are consistent with one GMPS tetramer of D<jats:sub>2<\/jats:sub> symmetry in the crystallographic asymmetric unit. Previously, GMPS has been observed only as a dimer in solution. GMPS was covalently modified with <jats:italic>p<\/jats:italic>\u2010chloromercuribenzylsulfonic acid (PCMBS), and its X\u2010ray fluorescence spectrum was measured through the L<jats:sub>III<\/jats:sub> absorption edge of mercury Anomalous scattering factors for cysteinyl mercury were derived from this spectrum, and the feasibility of structure determination by multi\u2010wavelength anomalous diffraction was evaluated. The optimal MAD dispersive signal is 4.5% of |<jats:italic>F<\/jats:italic>|, and the optimal MAD Bijvoet signal is 7.5% of |<jats:italic>F<\/jats:italic>| at a concentration of approximately 1 mercury per 10\u2010kDa protein. The anomalous scattering factors tabulated here should be transferable to cysteinyl mercury in other proteins. \u00a9 1994 John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/prot.340180410","type":"journal-article","created":{"date-parts":[[2005,5,29]],"date-time":"2005-05-29T01:33:07Z","timestamp":1117330387000},"page":"394-403","source":"Crossref","is-referenced-by-count":20,"title":["Preliminary x\u2010ray analysis of <i>Escherichia coli<\/i> GMP synthetase: Determination of anomalous scattering factors for a cysteinyl mercury derivative"],"prefix":"10.1002","volume":"18","author":[{"given":"John J. G.","family":"Tesmer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tim L.","family":"Stemmler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James E.","family":"Penner\u2010Hahn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.","family":"Jo Davisson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janet L.","family":"Smith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)99709-7"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00341a011"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)44840-0"},{"key":"e_1_2_1_5_2","doi-asserted-by":"crossref","first-page":"8676","DOI":"10.1016\/S0021-9258(17)39400-0","article-title":"Nucleotide sequence of the gua A gene encoding GMP synthetase of Escherichia coli K12","volume":"260","author":"Tiedeman A. A.","year":"1985","journal-title":"J. Biol. Chem."},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1002\/9780470123126.ch5"},{"key":"e_1_2_1_7_2","unstructured":"Smith J. 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J. H.","year":"1972","journal-title":"Eur. J. Biochem."},{"key":"e_1_2_1_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00162a062"},{"key":"e_1_2_1_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00014a001"},{"key":"e_1_2_1_20_2","doi-asserted-by":"publisher","DOI":"10.1103\/PhysRevB.44.4146"},{"key":"e_1_2_1_21_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja00161a051"},{"key":"e_1_2_1_22_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00752a016"},{"key":"e_1_2_1_23_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00523a005"},{"key":"e_1_2_1_24_2","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1016\/S0021-9258(19)86068-4","article-title":"Linkage between self\u2010association and catalytic activity of Escherichia coli. carbamoyl phosphate synthetase","volume":"255","author":"Powers S. G.","year":"1980","journal-title":"J. Biol. 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SERC Daresbury Laboratory Warrington U.K. 1991:96\u2013106."},{"key":"e_1_2_1_28_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0108767390005530"}],"container-title":["Proteins: Structure, Function, and Bioinformatics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fprot.340180410","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/prot.340180410","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,24]],"date-time":"2023-10-24T14:47:54Z","timestamp":1698158874000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/prot.340180410"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,4]]},"references-count":27,"journal-issue":{"issue":"4","published-print":{"date-parts":[[1994,4]]}},"alternative-id":["10.1002\/prot.340180410"],"URL":"https:\/\/doi.org\/10.1002\/prot.340180410","archive":["Portico"],"relation":{},"ISSN":["0887-3585","1097-0134"],"issn-type":[{"value":"0887-3585","type":"print"},{"value":"1097-0134","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,4]]}}}