X-ray diffraction images from ligand soaking experiment with protein crystal of Mtb-AnPRT

Main Author: Evans, Genevieve
Other Authors: Baker, Edward N. , Lott, J. Shaun
Format: Dataset
Terbitan: Mendeley , 2017
Subjects:
Online Access: https:/data.mendeley.com/datasets/xgn5z8jnr7
ctrlnum 0.17632-xgn5z8jnr7.1
fullrecord <?xml version="1.0"?> <dc><creator>Evans, Genevieve</creator><title>X-ray diffraction images from ligand soaking experiment with protein crystal of Mtb-AnPRT</title><publisher>Mendeley</publisher><description>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 153_1) corresponds to a ligand-free protein crystal treated with a 4 hour soak in cryoprotectant that contained 1 mM 8i, and this dataset was used to produce the protein structure PDB ID 5BO2. Also available is the auto-processed results generated at the Australian Synchrotron for this dataset.</description><subject>Crystallography</subject><subject>Structural Biology</subject><subject>Macromolecules</subject><subject>X-Ray Diffraction</subject><subject>Ligand Binding</subject><contributor>Baker, Edward N. </contributor><contributor>Lott, J. Shaun</contributor><type>Other:Dataset</type><identifier>10.17632/xgn5z8jnr7.1</identifier><rights>Creative Commons Attribution 4.0 International</rights><rights>http://creativecommons.org/licenses/by/4.0</rights><relation>https:/data.mendeley.com/datasets/xgn5z8jnr7</relation><date>2017-10-17T03:24:26Z</date><recordID>0.17632-xgn5z8jnr7.1</recordID></dc>
format Other:Dataset
Other
author Evans, Genevieve
author2 Baker, Edward N.
Lott, J. Shaun
title X-ray diffraction images from ligand soaking experiment with protein crystal of Mtb-AnPRT
publisher Mendeley
publishDate 2017
topic Crystallography
Structural Biology
Macromolecules
X-Ray Diffraction
Ligand Binding
url https:/data.mendeley.com/datasets/xgn5z8jnr7
contents 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 153_1) corresponds to a ligand-free protein crystal treated with a 4 hour soak in cryoprotectant that contained 1 mM 8i, and this dataset was used to produce the protein structure PDB ID 5BO2. Also available is the auto-processed results generated at the Australian Synchrotron for this dataset.
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institution Universitas Islam Indragiri
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