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Related Experiment Video

Updated: Jun 14, 2026

Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source

Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source

Published on: May 29, 2021

A rational approach to heavy-atom derivative screening.

M Gordon Joyce¹, Sergei Radaev, Peter D Sun

¹Structural Immunology Section, Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 12441 Parklawn Drive, Rockville, Maryland 20852, USA.

Acta Crystallographica. Section D, Biological Crystallography

|April 13, 2010

Summary

A new method streamlines heavy-atom derivative screening for protein structure determination, reducing trial-and-error and improving crystal quality for macromolecular phasing.

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Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source

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Published on: May 29, 2021

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Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin

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Published on: March 3, 2021

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Heavy-atom derivatization remains crucial for macromolecular phasing in protein structure determination.
Conventional methods are often inefficient due to trial-and-error, requiring numerous crystals and suffering from isomorphism issues.

Purpose of the Study:

To develop a rational, crystal-free screening method for heavy-atom derivatives.
To introduce a quick-soak derivatization procedure for efficient heavy-atom compound identification and improved phasing.

Main Methods:

Selection of reactive heavy-atom compounds based on protein-specific reactivity profiles.
Mass spectrometry screening to confirm protein-adduct formation.
Quick-soak derivatization to optimize crystal diffraction and isomorphism.

Main Results:

A streamlined workflow for identifying effective heavy-atom compounds.
Minimization of non-isomorphism issues, a common challenge in heavy-atom derivatization.
Enhanced diffraction quality from derivatized crystals.

Conclusions:

The developed system significantly improves the efficiency of heavy-atom derivative screening.
This approach overcomes key limitations of traditional heavy-atom methods in structural biology.
Facilitates more robust and high-throughput protein structure determination through improved phasing strategies.