Volume 91 Issue 48 | p. 29 | Concentrates
Issue Date: December 2, 2013

Protein Structure From Scratch

Free-electron laser X-ray source provides sufficiently accurate data to solve protein structures without need for additional information
Department: Science & Technology
Keywords: crystallography, protein structure, lysozyme, free-electron lasers
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A rendering of lysozyme.
Credit: Max Planck Society
A rendering of a ribbon structure of the protein lysozyme with two gadolinium atoms bound.
 
A rendering of lysozyme.
Credit: Max Planck Society

Free-electron lasers (FELs), which produce extremely intense, ultrashort X-ray pulses, have previously been used to determine structures of microscale protein crystals. But so far, all of the crystal structures solved this way have required the addition of data from already known and related structures. Now, researchers have used only FEL data to solve a known structure, lysozyme, at 2.1-Å resolution (Nature 2013, DOI: 10.1038/nature12773). Ilme Schlichting and Thomas R. M. Barends of the Max Planck Institute for Medical Research, in Heidelberg, Germany, and coworkers there and at SLAC National Accelerator Laboratory acquired diffraction images from a gadolinium derivative of lysozyme. They used the heavy atoms to align the images. The researchers collected more than 2.4 million images to obtain 60,000 images with usable data. The method is ready to move on to unknown protein structures, Barends says. “I would trust it just as much as any crystal structure determined using another X-ray source.” The method is particularly suited to proteins that are difficult to crystallize or are extremely sensitive to radiation damage.

 
Chemical & Engineering News
ISSN 0009-2347
Copyright © American Chemical Society

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