At the Deutsches Elektronen-Synchrotron (DESY), a research center of the Helmholtz Association in Germany, a team of scientists working within the newly built European X-Ray Free-Electron Laser Facility, have unveiled the structure of an enzyme involved in antibiotic resistance. While the finding is important in itself, it really validates a new instrument that will be critical at uncovering the structure of many proteins and other biological molecules.

In the new study, published in journal Nature Communications, the researchers describe their new X-ray laser that can produce pulses “with a megahertz inter-pulse spacing, more than four orders of magnitude higher than previously possible.” What’s interesting, is that while the technology was being built, it was not clear whether it would lead to quality imaging at such repetition rates. The first real test has demonstrated that indeed, the device does work as hoped for, imaging an already well understood lysozyme, as well as the not yet well studied complex of a β-lactamase from K. pneumoniae.

The three-diemnsional structure of the enzyme CTX-M-14 β-lactamase with the inhibitor avibactam bound to its active centre (green), as reconstructed from the measurements at the European XFEL. Credit: Universität Hamburg, Markus Perbandt

Study in Nature Communications: Megahertz serial crystallography…

Via: DESY…



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