skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

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

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 mm 3) 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 P2 12 12 1. 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.

Authors:
 [1];  [2];  [2];  [3];  [4];  [3]; ORCiD logo [3];  [2];  [1];  [2];  [1]
  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)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1334453
Grant/Contract Number:
AC05-00OR22725
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Acta Crystallographica. Section F, Structural Biology Communications
Additional Journal Information:
Journal Volume: 71; Journal Issue: 11; Journal ID: ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; lytic polysaccharide monooxygenase; chitin; Jonesia denitrificans; biofuel; neutron crystallography

Citation Formats

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., and Unkefer, Clifford J. Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase. United States: N. p., 2015. Web. doi:10.1107/S2053230X15019743.
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. Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase. United States. doi:10.1107/S2053230X15019743.
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., and Unkefer, Clifford J. Thu . "Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase". United States. doi:10.1107/S2053230X15019743. https://www.osti.gov/servlets/purl/1334453.
@article{osti_1334453,
title = {Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase},
author = {Bacik, John -Paul and Mekasha, Sophanit and Forsberg, Zarah and Kovalevsky, Andrey and Nix, Jay C. and Cuneo, Matthew J. and Coates, Leighton and Vaaje-Kolstad, Gustav and Chen, Julian C. -H. and Eijsink, Vincent G. H. and Unkefer, Clifford J.},
abstractNote = {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.},
doi = {10.1107/S2053230X15019743},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
number = 11,
volume = 71,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 2015},
month = {Thu Jan 01 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Citation Metrics:
Cited by: 2 works
Citation information provided by
Web of Science

Save / Share: