PETRA III pioneers protein serial crystallography at synchrotrons Using DESY’s synchrotron light source PETRA III, scientists have pioneered a new way to analyse delicate biomolecules. The novel approach, borrowed from a new class of high-intensity X-ray sources called free-electron lasers (FELs), could reveal the atomic structure of proteins that were previously inaccessible to synchrotrons, as the team led by Prof. Henry Chapman from the Hamburg Center for Free-Electron Laser Science CFEL reports in the scientific journal of the International Union of Crystallography, IUCrJ. CFEL is a joint institution of DESY, the University of Hamburg and the Max Planck Society. Electron density map of lysozyme at 2.1 Å resolution calculated from 40,233 single crystal indexed diffraction patterns. The atomic structure of biomolecules can reveal the mechanisms underlying their function in the organism, leading to improved biological insight with the potential to enable the development of new medicines. The standard technique for elucidating the atomic structure of proteins involves shining a bright beam of X-rays onto a protein crystal. The crystal scatters the X-rays in a characteristic way, and from the resulting diffraction pattern the inner structure of the crystal can be calculated, yielding the atomic structure of the protein. “But being jammed
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