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Title: Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase

Journal Article · · Acta Crystallographica. Section F, Structural Biology Communications
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  1. Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
  2. Norwegian Univ. of Life Sciences (Norway)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

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. As a result, 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.

Research Organization:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1334453
Journal Information:
Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue 11; ISSN 2053-230X
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 6 works
Citation information provided by
Web of Science

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Cited By (1)

Detection and Characterization of a Novel Copper‐Dependent Intermediate in a Lytic Polysaccharide Monooxygenase journal November 2019