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Related Experiment Video

Updated: Jun 25, 2026

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

Published on: June 17, 2021

Mini-beam collimator enables microcrystallography experiments on standard beamlines.

Robert F Fischetti¹, Shenglan Xu, Derek W Yoder

¹GM/CA CAT at the APS, Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA. rfischetti@anl.gov

Journal of Synchrotron Radiation

|February 26, 2009

Summary

A new mini-beam apparatus enables X-ray crystallography on smaller biological samples. This innovation allows researchers to solve challenging crystal structures previously unobtainable with standard X-ray beams.

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Area of Science:

Structural Biology
Crystallography
Synchrotron Radiation

Background:

High-brilliance X-ray beams from undulators are crucial for macromolecular crystallography.
Many important biological targets form crystals too small for standard X-ray beams (25-100 microm).
Existing microfocus beamlines were not optimized for macromolecular crystallography needs.

Purpose of the Study:

To develop a method for X-ray crystallography on biological samples smaller than 10 micrometers.
To enhance the capability of synchrotron beamlines for challenging structural targets.
To improve sample screening efficiency for macromolecular structure determination.

Main Methods:

Development of a 'mini-beam' apparatus to condition focused X-ray beams.
Implementation of a triple-collimator system for rapid beam size exchange.
Use of forward- and back-scatter guards to reduce background noise.

Main Results:

The mini-beam apparatus delivers focused beams of 5 or 10 micrometers (FWHM) with high intensity.
The mini-beam has a symmetric Gaussian shape and reduces vertical divergence by 25%.
Rapid interchange between focused and mini-beams facilitated sample screening and structure determination.

Conclusions:

The mini-beam apparatus significantly expands the scope of X-ray crystallography for small and inhomogeneous biological crystals.
This technology enables the structural analysis of previously inaccessible biological macromolecules and complexes.
The system's stability and rapid exchange capability enhance user efficiency at synchrotron facilities.