What is it about?
Protein crystals are usually 40 - 70% solvent and diffract X-rays weakly. Dehydrating protein crystals can decrease the solvent content and increase the quality of data that can be collected leading to a better model to understand the biology. In order to start dehydration the relative humidity that is equivalent to the liquid in which the crystal was grown must be found. Here we have provided a model to predict this.
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Why is it important?
Protein crystallography is essential in the understanding of fundamental biological processes and drug design. Methods that can improve the resolution of the data collected are therefore important. This model predicts the starting point for experiments that can improve protein crystals and also finds that most vapour diffusion experiments (the standard proceedure to produce protein crystals) are in fact batch as the difference on relative humidity is negligable.
Read the Original
This page is a summary of: Measurement of the equilibrium relative humidity for common precipitant concentrations: facilitating controlled dehydration experiments, Acta Crystallographica Section F Structural Biology and Crystallization Communications, December 2011, International Union of Crystallography,
DOI: 10.1107/s1744309111054029.
You can read the full text:
Resources
Inducing phase changes in crystals of macromolecules: Status and perspectives for controlled crystal dehydration
Description of how to perform dehydration experiments on protein crystals
Automation and Experience of Controlled Crystal Dehydration: Results from the European Synchrotron HC1 Collaboration
Description of results from a EU collaboration to determine how best to perform dehydration experiments.
Improving diffraction by humidity control: a novel device compatible with X-ray beamlines
A device to control the humidity surounding protein crystals is described
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