Evidence map›Paper›PMID 30511668›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.

Johannes Hermann, Phillip Nowotny, Tobias E Schrader, Philipp Biggel, Dariusch Hekmat, Dirk Weuster-Botz

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

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

0 citing papers in PubMed, 9 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 3 institutions in 1 country.

Johannes HermannInstitute of Biochemical Engineering, Technical University of Munich, Boltzmannstrasse 15, 85748 Garching, Germany.ORCID 0000-0003-2686-3771
Phillip NowotnyInstitute of Biochemical Engineering, Technical University of Munich, Boltzmannstrasse 15, 85748 Garching, Germany.ORCID 0000-0002-0767-1603
Tobias E SchraderJülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Centre (MLZ), Research Centre Jülich GmbH, Lichtenbergstrasse 1, 85748 Garching, Germany.ORCID 0000-0001-5159-0846
Philipp BiggelInstitute of Biochemical Engineering, Technical University of Munich, Boltzmannstrasse 15, 85748 Garching, Germany.
Dariusch HekmatInstitute of Biochemical Engineering, Technical University of Munich, Boltzmannstrasse 15, 85748 Garching, Germany.ORCID 0000-0003-0263-232X
Dirk Weuster-BotzInstitute of Biochemical Engineering, Technical University of Munich, Boltzmannstrasse 15, 85748 Garching, Germany.ORCID 0000-0002-1171-4194
Technical University of Munich · DEFischer (Germany) · DEHeinz Maier-Leibnitz Zentrum · DE

Funding

Deutsche Forschungsgemeinschaft WE2715/14-1
6 · The paper itself

Abstract

Lactobacillus brevis alcohol dehydrogenase (LbADH) is a well studied homotetrameric enzyme which catalyzes the enantioselective reduction of prochiral ketones to the corresponding secondary alcohols. LbADH is stable and enzymatically active at elevated temperatures and accepts a broad range of substrates, making it a valuable tool in industrial biocatalysis. Here, the expression, purification and crystallization of LbADH to generate large, single crystals with a volume of up to 1 mm

Indexed as

Alcohol DehydrogenaseAmino Acid SequenceBinding SitesCrystallography, X-RayHydrogen BondingLevilactobacillus brevisNeutron DiffractionProtein Structure, SecondaryProtein Structure, TertiaryAlcohol Dehydrogenasealcohol dehydrogenasehydrogen-bonding networkLactobacillus brevisneutron diffractionprotein crystallizationshort-chain dehydrogenases/reductases

Identifiers

PMID30511668
PMCPMC6277964
OpenAlexW2902471154

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.