Evidence map›Paper›PMID 38575747›Full record

ReviewNature protocols2024

Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins.

Rebeccah A Warmack, Belinda B Wenke, Thomas Spatzal, Douglas C Rees

Open access · greenAbstract readReview
In one paragraph

Review in Nature protocols, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
6.3field-weighted citation impact, top 4% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Rebeccah A WarmackDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA. rwarmack@caltech.edu.ORCID 0000-0002-9612-0511
Belinda B WenkeDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Thomas SpatzalDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.
Douglas C ReesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA. dcrees@caltech.edu.ORCID 0000-0003-4073-1185
California Institute of Technology · US

Funding

Crystallographic Studies of Electron Tranfer ProteinsR37GM045162 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REES, DOUGLAS CHARLES · 2003 to 2012
$3.1M
CRYSTALLOGRAPHIC STUDIES OF ELECTRON TRANSFER PROTEINSR01GM045162 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REES, DOUGLAS CHARLES · 1991 to 2018
$2.2M
In situ mechanisms of biological nitrogen fixationK99GM152765 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI WARMACK, REBECCAH · 2024 to 2025
$247k
Atomic Models of Nitrogen Fixation by Nitrogenase from CryoEM StructuresF32GM143836 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI WARMACK, REBECCAH · 2021 to 2022
$136k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM143836NIGMS NIH HHS K99 GM152765NIGMS NIH HHS R01 GM045162NIGMS NIH HHS R37 GM045162
6 · The paper itself

Abstract

Single-particle cryo-electron microscopy (cryoEM) provides an attractive avenue for advancing our atomic resolution understanding of materials, molecules and living systems. However, the vast majority of published cryoEM methodologies focus on the characterization of aerobically purified samples. Air-sensitive enzymes and microorganisms represent important yet understudied systems in structural biology. We have recently demonstrated the success of an anaerobic single-particle cryoEM workflow applied to the air-sensitive nitrogenase enzymes. In this protocol, we detail the use of Schlenk lines and anaerobic chambers to prepare samples, including a protein tag for monitoring sample exposure to oxygen in air. We describe how to use a plunge freezing apparatus inside of a soft-sided vinyl chamber of the type we routinely use for anaerobic biochemistry and crystallography of oxygen-sensitive proteins. Manual control of the airlock allows for introduction of liquid cryogens into the tent. A custom vacuum port provides slow, continuous evacuation of the tent atmosphere to avoid accumulation of flammable vapors within the enclosed chamber. These methods allowed us to obtain high-resolution structures of both nitrogenase proteins using single-particle cryoEM. The procedures involved can be generally subdivided into a 4 d anaerobic sample generation procedure, and a 1 d anaerobic cryoEM sample preparation step, followed by conventional cryoEM imaging and processing steps. As nitrogen is a substrate for nitrogenase, the Schlenk lines and anaerobic chambers described in this procedure are operated under an argon atmosphere; however, the system and these procedures are compatible with other controlled gas environments.

Indexed as

Cryoelectron MicroscopyNitrogenaseAirAnaerobiosisOxygenNitrogenaseOxygen

Identifiers

PMID38575747
PMCPMC11528890
OpenAlexW4393930013

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.