1oad
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Glucose isomerase from Streptomyces rubiginosus was crystallized in two, forms: I222, with one molecule of 44 kDa in the asymmetric unit, and, P2(1)2(1)2, with two unique molecules. The I222 structure is known, but, the P2(1)2(1)2 form has not been solved before. X-ray diffraction data for, the P2(1)2(1)2 form were collected at a wavelength of 1.54 A and data for, the I222 form were collected at three different wavelengths: 1.34, 1.07, and 0.98 A. The amount of anomalous signal from one Mn and eight S atoms, in these data sets varies from 1.24% to as low as 0.56%. The dual-space, direct-methods program SHELXD, run against the Bijvoet differences, gave a, clear solution of all anomalous scatterers for all data sets. The Mn, positions only were used for SAD phasing of all four data sets. ... | + | Glucose isomerase from Streptomyces rubiginosus was crystallized in two, forms: I222, with one molecule of 44 kDa in the asymmetric unit, and, P2(1)2(1)2, with two unique molecules. The I222 structure is known, but, the P2(1)2(1)2 form has not been solved before. X-ray diffraction data for, the P2(1)2(1)2 form were collected at a wavelength of 1.54 A and data for, the I222 form were collected at three different wavelengths: 1.34, 1.07, and 0.98 A. The amount of anomalous signal from one Mn and eight S atoms, in these data sets varies from 1.24% to as low as 0.56%. The dual-space, direct-methods program SHELXD, run against the Bijvoet differences, gave a, clear solution of all anomalous scatterers for all data sets. The Mn, positions only were used for SAD phasing of all four data sets. The, electron-density map after density modification, resulting from the, phasing of a single-wavelength data set and based purely on the anomalous, deltaf" contribution, was clearly interpretable; an almost complete model, of the protein was built by wARP without human intervention in all four, cases. As far as is known, this is the first time that an anomalous signal, as low as 0.6% has successfully been used to determine the structure of a, macromolecule. |
==About this Structure== | ==About this Structure== | ||
| - | 1OAD is a | + | 1OAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus] with MN, MG, MRD, MQD, TRS and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OAD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylose isomerase]] | [[Category: xylose isomerase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:19:21 2007'' |
Revision as of 12:14, 5 November 2007
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GLUCOSE ISOMERASE FROM STREPTOMYCES RUBIGINOSUS IN P21212 CRYSTAL FORM
Overview
Glucose isomerase from Streptomyces rubiginosus was crystallized in two, forms: I222, with one molecule of 44 kDa in the asymmetric unit, and, P2(1)2(1)2, with two unique molecules. The I222 structure is known, but, the P2(1)2(1)2 form has not been solved before. X-ray diffraction data for, the P2(1)2(1)2 form were collected at a wavelength of 1.54 A and data for, the I222 form were collected at three different wavelengths: 1.34, 1.07, and 0.98 A. The amount of anomalous signal from one Mn and eight S atoms, in these data sets varies from 1.24% to as low as 0.56%. The dual-space, direct-methods program SHELXD, run against the Bijvoet differences, gave a, clear solution of all anomalous scatterers for all data sets. The Mn, positions only were used for SAD phasing of all four data sets. The, electron-density map after density modification, resulting from the, phasing of a single-wavelength data set and based purely on the anomalous, deltaf" contribution, was clearly interpretable; an almost complete model, of the protein was built by wARP without human intervention in all four, cases. As far as is known, this is the first time that an anomalous signal, as low as 0.6% has successfully been used to determine the structure of a, macromolecule.
About this Structure
1OAD is a Single protein structure of sequence from Streptomyces rubiginosus with MN, MG, MRD, MQD, TRS and MPD as ligands. Active as Xylose isomerase, with EC number 5.3.1.5 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
SAD manganese in two crystal forms of glucose isomerase., Ramagopal UA, Dauter M, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):868-75. Epub 2003, Apr 25. PMID:12777803
Page seeded by OCA on Mon Nov 5 14:19:21 2007
Categories: Single protein | Streptomyces rubiginosus | Xylose isomerase | Dauter, M. | Dauter, Z. | Ramagopal, U.A. | MG | MN | MPD | MQD | MRD | TRS | Glucose isomerase | Isomerase
