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From Proteopedia
Crystal structure of Lymantria dispar CPV14 polyhedra 14 crystals
Structural highlights
FunctionPublication Abstract from PubMedVMXm joins the suite of operational macromolecular crystallography beamlines at Diamond Light Source. It has been designed to optimize rotation data collections from protein crystals less than 10 microm and down to below 1 microm in size. The beamline has a fully focused beam of 0.3 x 2.3 microm (vertical x horizontal) with a tuneable energy range (6-28 keV) and high flux (1.6 x 10(12) photons s(-1) at 12.5 keV). The crystals are housed within a vacuum chamber to minimize background scatter from air. Crystals are plunge-cooled on cryo-electron microscopy grids, allowing much of the liquid surrounding the crystals to be removed. These factors improve the signal-to-noise during data collection and the lifetime of the microcrystals can be prolonged by exploiting photoelectron escape. A novel in vacuo sample environment has been designed which also houses a scanning electron microscope to aid with sample visualization. This combination of features at VMXm allows measurements at the physical limits of X-ray crystallography on biomacromolecules to be explored and exploited. VMXm - A sub-micron focus macromolecular crystallography beamline at Diamond Light Source.,Warren AJ, Trincao J, Crawshaw AD, Beale EV, Duller G, Stallwood A, Lunnon M, Littlewood R, Prescott A, Foster A, Smith N, Rehm G, Gayadeen S, Bloomer C, Alianelli L, Laundy D, Sutter J, Cahill L, Evans G J Synchrotron Radiat. 2024 Nov 1;31(Pt 6):1593-1608. doi: , 10.1107/S1600577524009160. Epub 2024 Oct 30. PMID:39475835[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Lymantria dispar | Crawshaw A | Evans G | Stuart D | Sutton G | Trincao J | Warren A