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- Title
Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase.
- Authors
Bacik, John-Paul; Mekasha, Sophanit; Forsberg, Zarah; Kovalevsky, Andrey; Nix, Jay C.; Cuneo, Matthew J.; Coates, Leighton; Vaaje-Kolstad, Gustav; Chen, Julian C.-H.; Eijsink, Vincent G. H.; Unkefer, Clifford J.
- Abstract
Bacteria and fungi express lytic polysaccharide monooxgyenase (LPMO) enzymes that act in conjunction with canonical hydrolytic sugar-processing enzymes to rapidly convert polysaccharides such as chitin, cellulose and starch to single monosaccharide products. In order to gain a better understanding of the structure and oxidative mechanism of these enzymes, large crystals (1-3 mm3) of a chitin-processing LPMO from the Gram-positive soil bacterium Jonesia denitrificans were grown and screened for their ability to diffract neutrons. In addition to the collection of neutron diffraction data, which were processed to 2.1 Å resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1 Å resolution in space group P212121. To our knowledge, this work marks the first successful neutron crystallographic experiment on an LPMO. Joint X-ray/neutron refinement of the resulting data will reveal new details of the structure and mechanism of this recently discovered class of enzymes.
- Subjects
NEUTRONS; POLYSACCHARIDES; MONOOXYGENASES
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2015, Vol 71, Issue 11, p1448
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X15019743