Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups

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Journal Article
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Language
English
Date
2017
Authors
Evans GL
Furkert DP
Abermil N
Kundu P
de Lange KM
Parker EJ
Brimble MA
Baker EN
Lott JS
Abstract

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. P2 1 , C2, P2 1 2 1 2, P2 1 2 1 2 1 ). This article outlines experimental details for 3 additional Mtb-AnPRT:inhibitor structures. For one protein:inhibitor complex, two datasets are presented – 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.

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Keywords
Crystallography, Ligand binding, Macromolecules, Structure-based inhibitor design, X-ray diffraction
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ANZSRC fields of research
Field of Research::03 - Chemical Sciences::0304 - Medicinal and Biomolecular Chemistry
Rights
Copyright 2017 TheAuthors. Published by Elsevier Inc.This is an open access article under the CCBY license (http://creativecommons.org/licenses/by/4.0/).