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Crystallization and preliminary X-ray analysis of Escherichia coli GlnK
The trimeric signal‐transduction protein GlnK, from Escherichia coli, has been over‐expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 Å and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63...
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Published in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-09, Vol.54 (5), p.996-998 |
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container_issue | 5 |
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container_title | Acta crystallographica. Section D, Biological crystallography. |
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creator | Macpherson, Kirsty H. R. Xu, Yibin Cheah, Eong Carr, Paul D. Van Heeswijk, Wally C. Westerhoff, Hans V. Luque, Eva Vasudevan, Subhash G. Ollis, David L. |
description | The trimeric signal‐transduction protein GlnK, from Escherichia coli, has been over‐expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 Å and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 Å and c = 54.79 Å. These crystals have a single subunit in the asymmetric unit. High‐quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 Å. |
doi_str_mv | 10.1107/S0907444998001887 |
format | article |
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High‐quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 Å.</description><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - enzymology</subject><subject>Protein Conformation</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Signal Transduction</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkE1LAzEQhoMoWqs_wIOwJ2-r-dh8HUtbt2pRQUU9hWw2i9F0tyYtuv56t7SI4MHTDPPO8zLzAnCE4ClCkJ_dQQl5lmVSCgiREHwL9BCRMoUw49u_-j2wH-MrhBBjwnfBruSUIyR6IB-GNi609-5LL1xTJ7ouk3mw3s1crUObPKVBt91U-za6mDRVMo7mxQZnXpxOTONdkvv66gDsVNpHe7ipffBwPr4fTtLpTX4xHExTQwSRqamohZgzhjNUZaYqCkol0xoXVkpLTYZEiWlpmMFYsMwwhEkpq4oYinlBJOmDk7XvPDTvSxsXauaisd7r2jbLqJiUVEBKu0W0XjShiTHYSs2Dm3UfKQTVKjz1J7yOOd6YL4uZLX-ITVqdLtb6h_O2_d9QDZ5HkwFEbHV3ukZdXNjPH1SHN8U44VQ9Xucqf6T8luBLNSLfsZ2Icw</recordid><startdate>19980901</startdate><enddate>19980901</enddate><creator>Macpherson, Kirsty H. 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source | Wiley-Blackwell Read & Publish Collection; Alma/SFX Local Collection |
subjects | Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Carrier Proteins - chemistry Carrier Proteins - isolation & purification Crystallization Crystallography, X-Ray Escherichia coli - enzymology Protein Conformation Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification Signal Transduction |
title | Crystallization and preliminary X-ray analysis of Escherichia coli GlnK |
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