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

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 o...

Full description

Saved in:
Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2015-11, Vol.71 (11), p.1448-1452
Main 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.
Format: Article
Language:English
Subjects:
Bacteria
BASIC BIOLOGICAL SCIENCES
biofuel
chitin
Crystallization
Crystallography
Crystallography, X-Ray
Diffraction
Enzymes
Fungi
Gram-Positive Bacteria - enzymology
Jonesia denitrificans
lytic polysaccharide monooxygenase
Mixed Function Oxygenases - chemistry
Mixed Function Oxygenases - isolation & purification
neutron crystallography
Neutron diffraction
Neutron Diffraction - methods
Polysaccharides
Polysaccharides, Bacterial - chemistry
Polysaccharides, Bacterial - isolation & purification
Research Communications
Temperature
X-rays
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X15019743