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Related Experiment Video

Updated: Apr 28, 2026

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

A new view on crystal harvesting.

Joseph R Luft¹, Thomas D Grant¹, Jennifer R Wolfley¹

¹Hauptman-Woodward Medical Research Institute, 700 Ellicott Street, Buffalo, NY 14203, USA.

Journal of Applied Crystallography

|June 7, 2014

Summary

This study introduces an inverted microscopy method for easier crystal handling in X-ray crystallography. This technique facilitates the structural analysis of challenging protein samples, improving high-throughput screening outcomes.

Keywords:

crystal imaging crystal mounting high throughput

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Area of Science:

Structural biology
Biochemistry
Crystallography

Background:

X-ray crystallography requires crystal mounting, which is challenging for small samples near microscope objectives.
Current methods hinder manipulation and harvesting of crystals in microplates.

Purpose of the Study:

To develop an improved method for crystal manipulation and harvesting in X-ray crystallography.
To overcome limitations in handling small crystals during high-throughput screening.

Main Methods:

Inverted microscopy approach: moving the objective lens to the bottom of a clear crystallization plate.
Crystal harvesting from 0.9 mm diameter, 5.0 mm depth wells.
Application to structural solution of *Saccharomyces cerevisiae* glutaminyl-tRNA synthetase.

Main Results:

Successfully manipulated and harvested crystals using the inverted view.
Enabled structural solution of a recalcitrant protein domain (187 amino acid N-terminal domain of *S. cerevisiae* glutaminyl-tRNA synthetase).
Demonstrated feasibility for crystals from high-throughput screening.

Conclusions:

Inverted microscopy simplifies crystal manipulation and harvesting for X-ray crystallography.
This method facilitates structural studies of proteins identified in high-throughput screening.
The approach enhances manual and automated crystal handling processes.