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 Video

Updated: Jun 16, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

PHENIX: a comprehensive Python-based system for macromolecular structure solution.

Paul D Adams1, Pavel V Afonine, Gábor Bunkóczi

  • 1Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. pdadams@lbl.gov

Acta Crystallographica. Section D, Biological Crystallography
|February 4, 2010
PubMed
Summary

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

Scotty: lattice coincidences for macromolecular crystallographic phasing.

Acta crystallographica. Section D, Structural biology·2026
Same author

Scotty: lattice coincidences in the Protein Data Bank.

Acta crystallographica. Section D, Structural biology·2026
Same author

PRIME: An evaluation framework for protein representation inference and generalization in viral mutation space.

BMC genomics·2026
Same author

RNAprecis: Prediction of full-detail RNA conformation from the experimentally best-observed sparse parameters.

PLoS computational biology·2026
Same author

Discovering novel therapeutic V<sub>H</sub>Hs for emerging viruses: perspectives from VEEV selection strategies.

Frontiers in immunology·2026
Same author

A Chimeric LBT-GFP Biosensor Exhibits Antithetical Fluorescence Responses to Ca<sup>2+</sup> and Dy<sup>3+</sup> Binding.

ACS omega·2026
Same journal

Structural insights into the synthesis of FMN in prokaryotic organisms.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Native sulfur/chlorine SAD phasing for serial femtosecond crystallography.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Serial crystallographic analysis of protein isomorphous replacement data from a mixture of native and derivative microcrystals.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

The first crystal structure of the peptidase domain of the U32 peptidase family.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.

Acta crystallographica. Section D, Biological crystallography·2015
Same journal

Structural characterization of a mitochondrial 3-ketoacyl-CoA (T1)-like thiolase from Mycobacterium smegmatis.

Acta crystallographica. Section D, Biological crystallography·2015
See all related articles
This summary is machine-generated.

Automating macromolecular X-ray crystallography (MX) structure solution, PHENIX minimizes manual data interpretation. This comprehensive system enhances efficiency in understanding biological processes at the molecular level.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Macromolecular X-ray crystallography (MX) is crucial for understanding molecular-level biological processes.
  • Current MX methods often require extensive manual data interpretation and software use, demanding significant time and effort.
  • Challenges in structure solution hinder the rapid advancement of molecular biology research.

Purpose of the Study:

  • To develop a comprehensive system for automated macromolecular crystallographic structure solution.
  • To reduce the reliance on manual interpretation and subjective input in X-ray crystallography.
  • To streamline and integrate traditionally separate procedures in structure determination.

Main Methods:

  • Development of algorithms to minimize subjective input in data analysis.

More Related Videos

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

Related Experiment Videos

Last Updated: Jun 16, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Modeling Ligands into Maps Derived from Electron Cryomicroscopy
09:30

Modeling Ligands into Maps Derived from Electron Cryomicroscopy

Published on: July 19, 2024

  • Implementation of automated procedures for tasks traditionally done manually.
  • Creation of an integrated framework for seamless algorithm execution.

    • Main Results:

    • PHIENIX provides a comprehensive system for macromolecular structure solution.
    • Automation significantly reduces the time and effort required for X-ray crystallography.
    • Minimized subjective input leads to more objective and reproducible results.

    Conclusions:

    • PHIENIX offers an automated and integrated approach to macromolecular X-ray crystallography.
    • The system enhances efficiency and objectivity in solving complex molecular structures.
    • This advancement facilitates a deeper understanding of biological processes through structural biology.