Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups
There are twenty-five published structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) that use the same crystallization protocol. The structures include protein complexed with natural and alternative substrates, protein:inhibitor complexes, and variants with mut...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2017-12-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340917305723 |
| _version_ | 1828531780177625088 |
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| author | Genevieve L. Evans Daniel P. Furkert Nacim Abermil Preeti Kundu Katrina M. de Lange Emily J. Parker Margaret A. Brimble Edward N. Baker J. Shaun Lott |
| author_facet | Genevieve L. Evans Daniel P. Furkert Nacim Abermil Preeti Kundu Katrina M. de Lange Emily J. Parker Margaret A. Brimble Edward N. Baker J. Shaun Lott |
| author_sort | Genevieve L. Evans |
| collection | DOAJ |
| description | There are twenty-five published structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) that use the same crystallization protocol. The structures include protein complexed with natural and alternative substrates, protein:inhibitor complexes, and variants with mutations of substrate-binding residues. Amongst these are varying space groups (i.e. P21, C2, P21212, P212121). This article outlines experimental details for 3 additional Mtb-AnPRT:inhibitor structures. For one protein:inhibitor complex, two datasets are presented â one generated by crystallization of protein in the presence of the inhibitor and another where a protein crystal was soaked with the inhibitor. Automatic and manual processing of these datasets indicated the same space group for both datasets and thus indicate that the space group differences between structures of Mtb-AnPRT:ligand complexes are not related to the method used to introduce the ligand. Keywords: Crystallography, Macromolecules, X-ray diffraction, Ligand binding, Structure-based inhibitor design |
| first_indexed | 2024-12-11T22:43:32Z |
| format | Article |
| id | doaj.art-5c6539f806014fd3a63a51b4a3d201bc |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-11T22:43:32Z |
| publishDate | 2017-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-5c6539f806014fd3a63a51b4a3d201bc2022-12-22T00:47:43ZengElsevierData in Brief2352-34092017-12-011510191029Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groupsGenevieve L. Evans0Daniel P. Furkert1Nacim Abermil2Preeti Kundu3Katrina M. de Lange4Emily J. Parker5Margaret A. Brimble6Edward N. Baker7J. Shaun Lott8Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New Zealand; Corresponding author. Present address:Â KU Leuven, Laboratory for Structural Neurobiology, Department of Cellular and Molecular Medicine, Herestraat 49, P.O. Box 601, B-3000 Leuven, BelgiumMaurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, P.O. Box 4800, Christchurch 8140, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, P.O. Box 4800, Christchurch 8140, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New ZealandMaurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New Zealand; Corresponding author.There are twenty-five published structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) that use the same crystallization protocol. The structures include protein complexed with natural and alternative substrates, protein:inhibitor complexes, and variants with mutations of substrate-binding residues. Amongst these are varying space groups (i.e. P21, C2, P21212, P212121). This article outlines experimental details for 3 additional Mtb-AnPRT:inhibitor structures. For one protein:inhibitor complex, two datasets are presented â one generated by crystallization of protein in the presence of the inhibitor and another where a protein crystal was soaked with the inhibitor. Automatic and manual processing of these datasets indicated the same space group for both datasets and thus indicate that the space group differences between structures of Mtb-AnPRT:ligand complexes are not related to the method used to introduce the ligand. Keywords: Crystallography, Macromolecules, X-ray diffraction, Ligand binding, Structure-based inhibitor designhttp://www.sciencedirect.com/science/article/pii/S2352340917305723 |
| spellingShingle | Genevieve L. Evans Daniel P. Furkert Nacim Abermil Preeti Kundu Katrina M. de Lange Emily J. Parker Margaret A. Brimble Edward N. Baker J. Shaun Lott Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups Data in Brief |
| title | Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups |
| title_full | Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups |
| title_fullStr | Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups |
| title_full_unstemmed | Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups |
| title_short | Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups |
| title_sort | datasets processing and refinement details for mtb anprt inhibitor structures with various space groups |
| url | http://www.sciencedirect.com/science/article/pii/S2352340917305723 |
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