What is it about?
Determining the structure of molecules and proteins is important for understanding how they interact with the body. This is usually done with crystallography, where a single large crystal is grown and rotated in an X-ray beam, and the diffracted intensity is used to determine the structure. For various reasons, it can be hard to grow large crystals. Here we present a method of getting the crystal structure using fluctuation scattering, which can be used with lots of small crystals in random orientations, rather than a single large crystal that is rotated.
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Photo by Evgeniya Shustikova on Unsplash
Why is it important?
Modern serial crystallography techniques already utilize the scattering of many individual single crystals to determine structure. Correlation analysis can be used in this case, and in the case for multiple crystals scattering at once. Some molecules and proteins, such as membrane proteins, do not readily crystalize into large single crystals. This method could aid in determining the structure of these challenging proteins.
Perspectives
This article represents a major outcome of my PhD thesis, and I am very proud of the work that my supervisors and myself have put into it. I hope that the readers find as much use and interest in this work as I had joy in creating it.
Patrick Adams
RMIT University
Read the Original
This page is a summary of: Crystal structure via fluctuation scattering, IUCrJ, June 2024, International Union of Crystallography,
DOI: 10.1107/s2052252524003932.
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