X-ray diffraction images for the protein Mtb-AnPRT crystallised in the presence of the ligand

Published: 17 October 2017| Version 1 | DOI: 10.17632/2zrfgv34nb.1
Genevieve Evans, Edward N. Baker, J. Shaun Lott


Two macromolecular X-ray diffraction datasets were collected that correspond to co-crystal and soaking experiments with the same ligand and protein. X-ray diffraction images were collected at the Australian Synchrotron on the MX1 beamline on March 25th, 2015. Regardless of the manner the ligand was introduced, both datasets were found to process with the same space group (C2) and could be subquently solved using molecular replacement. The protein Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) used in this study had previously been found to process in four different space groups (e.g. P21, C2, P21212, and P212121). The ligand utilised in these experiments was a Mtb-AnPRT inhibitor, 2-(2-carboxyphenylamino)-5-(3-phosphonopropoxy)benzoic acid (annotated as 8i). This inhibitor is similar to one of the enzyme's substrates -- i.e. bianthranilate-like. This substrate-like component was meant to act as an "anchor" with the compound also containing a 4-atom "line" and phosphonate "hook". This X-ray diffraction dataset (annotated 154_10) corresponds to protein co-crystallized in presence of 1 mM 8i. Also available is the auto-processed results generated at the Australian Synchrotron for this dataset.


Steps to reproduce

Details of the experimental method can be found in the Data-in-Brief article entitled: "Datasets, processing and refinement details for Mtb-AnPRT:inhibitors structures with various space groups"


Australian Synchrotron Co Ltd, University of Auckland


Crystallography, Structural Biology, Macromolecules, X-Ray Diffraction, Ligand Binding