Evidence map›Paper›PMID 26527275›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

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 and 1 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 33% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 2 countries.

John Paul BacikProtein Crystallography Station, Bioscience Division, Los Alamos National Laboratory, TA-03, Bldg 4200, MS T007, Los Alamos, NM 87545, USA.
Sophanit MekashaDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO Box 5003, 1430 Ås, Norway.
Zarah ForsbergDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO Box 5003, 1430 Ås, Norway.
Andrey KovalevskyBiology and Soft Matter Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, PO Box 2008, Oak Ridge, NM 37831, USA.
Jay C NixAdvanced Light Source, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA.
Matthew J CuneoBiology and Soft Matter Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, PO Box 2008, Oak Ridge, NM 37831, USA.
Leighton CoatesBiology and Soft Matter Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, PO Box 2008, Oak Ridge, NM 37831, USA.
Gustav Vaaje-KolstadDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO Box 5003, 1430 Ås, Norway.
Julian C H ChenProtein Crystallography Station, Bioscience Division, Los Alamos National Laboratory, TA-03, Bldg 4200, MS T007, Los Alamos, NM 87545, USA.
Vincent G H EijsinkDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO Box 5003, 1430 Ås, Norway.
Clifford J UnkeferProtein Crystallography Station, Bioscience Division, Los Alamos National Laboratory, TA-03, Bldg 4200, MS T007, Los Alamos, NM 87545, USA.
Norwegian University of Life Sciences · NOLos Alamos National Laboratory · USOak Ridge National Laboratory · USLawrence Berkeley National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 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.

Indexed as

CrystallizationCrystallography, X-RayGram-Positive BacteriaMixed Function OxygenasesNeutron DiffractionPolysaccharides, BacterialTemperatureMixed Function OxygenasesPolysaccharides, BacterialbiofuelchitinJonesia denitrificanslytic polysaccharide monooxygenaseneutron crystallography

Identifiers

PMID26527275
PMCPMC4631597
OpenAlexW1958829939

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.