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

John Paul Bacik; Sophanit Mekasha; Zarah Forsberg; Andrey Kovalevsky; Jay C. Nix; Matthew J. Cuneo; Leighton Coates; Gustav Vaaje-Kolstad; Julian C.H. Chen; Vincent G.H. Eijsink; Clifford J. Unkefer

doi:10.1107/S2053230X15019743

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

John Paul Bacik, Sophanit Mekasha, Zarah Forsberg, Andrey Kovalevsky, Jay C. Nix, Matthew J. Cuneo, Leighton Coates, Gustav Vaaje-Kolstad, Julian C.H. Chen, Vincent G.H. Eijsink, Clifford J. Unkefer

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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 (1-3mm³) 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 2.1Å resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1Å 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.

Original language	English
Pages (from-to)	1448-1452
Number of pages	5
Journal	Acta Crystallographica Section F:Structural Biology Communications
Volume	71
DOIs	https://doi.org/10.1107/S2053230X15019743
State	Published - 2015

Keywords

Jonesia denitrificans
biofuel
chitin
lytic polysaccharide monooxygenase
neutron crystallography

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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Bacik, J. P., Mekasha, S., Forsberg, Z., Kovalevsky, A., Nix, J. C., Cuneo, M. J., Coates, L., Vaaje-Kolstad, G., Chen, J. C. H., Eijsink, V. G. H., & Unkefer, C. J. (2015). Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase. Acta Crystallographica Section F:Structural Biology Communications, 71, 1448-1452. https://doi.org/10.1107/S2053230X15019743

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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 (1-3mm3) 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{\AA} resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1{\AA} 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.",

keywords = "Jonesia denitrificans, biofuel, chitin, lytic polysaccharide monooxygenase, neutron crystallography",

author = "Bacik, {John Paul} and Sophanit Mekasha and Zarah Forsberg and Andrey Kovalevsky and Nix, {Jay C.} and Cuneo, {Matthew J.} and Leighton Coates and Gustav Vaaje-Kolstad and Chen, {Julian C.H.} and Eijsink, {Vincent G.H.} and Unkefer, {Clifford J.}",

note = "Publisher Copyright: {\textcopyright} 2015 International Union of Crystallography.",

year = "2015",

doi = "10.1107/S2053230X15019743",

language = "English",

volume = "71",

pages = "1448--1452",

journal = "Acta Crystallographica Section F:Structural Biology Communications",

issn = "2053-230X",

publisher = "International Union of Crystallography",

}

Bacik, JP, Mekasha, S, Forsberg, Z, Kovalevsky, A, Nix, JC, Cuneo, MJ, Coates, L, Vaaje-Kolstad, G, Chen, JCH, Eijsink, VGH & Unkefer, CJ 2015, 'Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase', Acta Crystallographica Section F:Structural Biology Communications, vol. 71, pp. 1448-1452. https://doi.org/10.1107/S2053230X15019743

TY - JOUR

T1 - Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase

AU - Bacik, John Paul

AU - Mekasha, Sophanit

AU - Forsberg, Zarah

AU - Kovalevsky, Andrey

AU - Nix, Jay C.

AU - Cuneo, Matthew J.

AU - Coates, Leighton

AU - Vaaje-Kolstad, Gustav

AU - Chen, Julian C.H.

AU - Eijsink, Vincent G.H.

AU - Unkefer, Clifford J.

PY - 2015

Y1 - 2015

N2 - 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 (1-3mm3) 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 2.1Å resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1Å 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.

AB - 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 (1-3mm3) 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 2.1Å resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1Å 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.

KW - Jonesia denitrificans

KW - biofuel

KW - chitin

KW - lytic polysaccharide monooxygenase

KW - neutron crystallography

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U2 - 10.1107/S2053230X15019743

DO - 10.1107/S2053230X15019743

M3 - Article

C2 - 26527275

AN - SCOPUS:84946556616

SN - 2053-230X

VL - 71

SP - 1448

EP - 1452

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

ER -

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

Abstract

Keywords

UN SDGs

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