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Related Experiment Video

Updated: Jun 16, 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

'Hot' macromolecular crystals.

Katarzyna D Koclega¹, Maksymilian Chruszcz, Matthew D Zimmerman

¹Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.

Crystal Growth & Design

|February 18, 2010

Summary

This summary is machine-generated.

Crystallizing proteins like TM1030 at various temperatures, including elevated ones, yielded high-quality crystals. This suggests exploring a broader temperature range in crystallization protocols can improve protein structure determination.

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Harvesting and Cryo-cooling Crystals of Membrane Proteins Grown in Lipidic Mesophases for Structure Determination by Macromolecular Crystallography

Harvesting and Cryo-cooling Crystals of Membrane Proteins Grown in Lipidic Mesophases for Structure Determination by Macromolecular Crystallography

Published on: September 2, 2012

Area of Science:

Structural biology
Protein crystallography
Biophysics

Background:

Hyperthermophilic proteins present unique crystallization challenges.
Understanding protein-DNA complex structures is crucial for molecular biology.
The Protein Data Bank (PDB) underrepresents structures determined at elevated temperatures.

Purpose of the Study:

To investigate the effect of crystallization temperature on protein crystal quality.
To assess the stability and diffraction of TM1030-DNA complex crystals grown at different temperatures.
To evaluate the potential of elevated temperatures as a standard crystallization parameter.

Main Methods:

Crystallization of TM1030 and its DNA complex across a temperature range (4°C, 20°C, 37°C, 50°C).
X-ray diffraction experiments on crystals grown at various temperatures.
Comparison of structural models derived from differently grown crystals.

Main Results:

Optimal crystals for the TM1030-DNA complex were obtained at 4°C, 20°C, and 37°C.
TM1030 alone crystallized effectively across all tested temperatures.
Structural models from crystals grown at different temperatures showed comparable quality.

Conclusions:

Protein crystals can be successfully grown and remain stable over a wide temperature range.
Elevated temperature crystallization is a viable method for obtaining high-quality protein structures.
Incorporating elevated temperature screening into standard protocols may enhance crystallization success rates.