Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Membrane lipid composition: an important but neglected aspect of membrane protein simulation.

Physical chemistry chemical physics : PCCP·2026
Same author

Ancestral neuronal receptors are bacterial accessory toxins.

Nature communications·2026
Same author

Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.

Nature communications·2025
Same author

PDBe: enhanced structural data exploration to facilitate discovery.

Nucleic acids research·2025
Same author

Protease mimicry: Dissecting the ester bond crosslinking mechanics in bacterial adhesin proteins.

Protein science : a publication of the Protein Society·2025
Same author

Mechanistic Insights into Homoserine <i>O</i>-Acetyltransferase from <i>Mycobacterium tuberculosis</i>.

Biochemistry·2025

Related Experiment Video

Updated: Feb 18, 2026

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

7.3K

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

Genevieve L Evans1, Daniel P Furkert2, Nacim Abermil2

  • 1Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3 Symonds Street, Auckland 1142, New Zealand.

Data in Brief
|November 24, 2017
PubMed
Summary

This study details new Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) structures. Ligand introduction methods do not affect Mtb-AnPRT crystal space groups, clarifying structural variability.

Keywords:
CrystallographyLigand bindingMacromoleculesStructure-based inhibitor designX-ray diffraction

More Related Videos

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

5.7K
Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

2.2K

Related Experiment Videos

Last Updated: Feb 18, 2026

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

7.3K
Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

5.7K
Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
09:30

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps

Published on: July 19, 2024

2.2K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Twenty-five structures of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase (Mtb-AnPRT) exist, utilizing a consistent crystallization protocol.
  • These structures encompass various states: complexed with natural/alternative substrates, bound to inhibitors, and featuring mutations in substrate-binding residues.
  • Observed variations in space groups (P21, C2, P21212, P212121) among published Mtb-AnPRT structures suggest potential influences on crystal packing.

Purpose of the Study:

  • To present experimental details for three additional Mtb-AnPRT:inhibitor structures.
  • To investigate the impact of ligand introduction methods on the observed space groups of Mtb-AnPRT crystals.
  • To clarify whether differences in space groups are attributable to crystallization versus soaking techniques for ligand incorporation.

Main Methods:

  • X-ray crystallography was employed to determine the structures of Mtb-AnPRT in complex with inhibitors.
  • Two distinct methods for introducing the inhibitor were utilized for one complex: co-crystallization and crystal soaking.
  • Both automatic and manual data processing techniques were applied to analyze the crystallographic datasets.

Main Results:

  • Three new Mtb-AnPRT:inhibitor structures were detailed.
  • Analysis of datasets from both co-crystallization and soaking methods for a specific complex yielded the same space group.
  • This finding indicates that the method of ligand introduction does not influence the resulting space group.

Conclusions:

  • The space group of Mtb-AnPRT crystals is independent of whether the ligand is incorporated during crystallization or via soaking.
  • This resolves ambiguity regarding the cause of differing space groups observed in previously published Mtb-AnPRT structures.
  • The study provides a clearer understanding of Mtb-AnPRT structural variability and aids in the interpretation of existing and future crystallographic data.