Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups
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
Affiliations
Genevieve L. Evans
Maurice 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, Belgium
Daniel P. Furkert
Maurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New Zealand
Nacim Abermil
Maurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New Zealand
Preeti Kundu
Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, P.O. Box 4800, Christchurch 8140, New Zealand
Katrina M. de Lange
Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New Zealand
Emily J. Parker
Maurice Wilkins Centre for Molecular Biodiscovery, Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, P.O. Box 4800, Christchurch 8140, New Zealand
Margaret A. Brimble
Maurice Wilkins Centre for Molecular Biodiscovery and School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1142, New Zealand
Edward N. Baker
Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New Zealand
J. Shaun Lott
Maurice 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 design
