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 Experiment Videos

In-house low-resolution X-ray crystallography.

G Evans1, P Roversi, G Bricogne

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England. gwyndaf@mrc-lmb.cam.ac.uk

Acta Crystallographica. Section D, Biological Crystallography
|September 22, 2000
PubMed
Summary
This summary is machine-generated.

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

Observation of WWW Production in pp Collisions at sqrt[s]=13  TeV with the ATLAS Detector.

Physical review letters·2022
Same author

Search for Lepton-Flavor Violation in Z-Boson Decays with τ Leptons with the ATLAS Detector.

Physical review letters·2022
Same author

Search for New Phenomena in Final States with Two Leptons and One or No b-Tagged Jets at sqrt[s]=13  TeV Using the ATLAS Detector.

Physical review letters·2021
Same author

Search for Displaced Leptons in sqrt[s]=13  TeV pp Collisions with the ATLAS Detector.

Physical review letters·2021
Same author

Effects of breeding history and crop management on the root architecture of wheat.

Plant and soil·2020
Same author

A Novel, Enriched Population Pharmacokinetic Model for Recombinant Factor VIII-Fc Fusion Protein Concentrate in Hemophilia A Patients.

Thrombosis and haemostasis·2020

Standard X-ray diffraction equipment can be modified for low-resolution macromolecular crystallography. This enables accurate data collection for determining molecular envelopes and analyzing large, weakly diffracting crystals in-house.

Area of Science:

  • Structural Biology
  • Crystallography
  • Biophysics

Background:

  • X-ray diffraction is crucial for determining macromolecular structures.
  • Collecting low-resolution data from challenging samples can be difficult with standard equipment.

Purpose of the Study:

  • To demonstrate that standard in-house X-ray diffraction apparatus can be modified for low-resolution crystallography.
  • To assess the utility of modified in-house systems for analyzing macromolecular samples.

Main Methods:

  • Modification of standard in-house protein crystal X-ray diffraction apparatus.
  • Collection of very low-resolution diffraction data.
  • Contrast-variation measurements on lysozyme crystals.
  • Diffraction measurements on 30S ribosomal subunit crystals.

Related Experiment Videos

Main Results:

  • Successful measurement of very low-resolution reflections with modified in-house apparatus.
  • Acquisition of accurate data for macromolecular envelope determination using lysozyme.
  • Demonstration of data collection from small, weakly diffracting 30S ribosome subunit crystals.

Conclusions:

  • Modified in-house X-ray diffraction systems are effective for low-resolution macromolecular crystallography.
  • These methods provide valuable data for structural envelope determination and analysis of large, challenging macromolecules.