Evidence map›Paper›PMID 38411550›Full record

ArticleActa crystallographica. Section D, Structural biology2024

XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.

Joshua A Hull, Cheol Lee, Jin Kyun Kim, Seon Woo Lim, Jaehyun Park, Sehan Park, Sang Jae Lee, Gisu Park, Intae Eom, Minseok Kim and 6 more

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
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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

16 authors.

Joshua A HullDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Cheol LeeDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.ORCID 0000-0002-3939-2457
Jin Kyun KimDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Seon Woo LimDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Jaehyun ParkPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.
Sehan ParkPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.
Sang Jae LeePohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.
Gisu ParkPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.ORCID 0000-0002-4368-8840
Intae EomPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.
Minseok KimPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.ORCID 0000-0002-2504-1314
HyoJung HyunPohang Accelerator Laboratory, POSTECH, Pohang 37673, Republic of Korea.ORCID 0000-0002-3930-551X
Jacob E CombsDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Jacob T AndringDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.ORCID 0000-0002-6632-6391
Carrie LomelinoDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Chae Un KimDepartment of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.ORCID 0000-0001-9350-8441
Robert McKennaDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.

Funding

National Research Foundation of Korea 2022R1A2C2091815
6 · The paper itself

Abstract

The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO

Indexed as

Carbonic Anhydrase IICrystallography, X-RayHumansProteinsSynchrotronsX-RaysCarbonic Anhydrase IIProteinscarbonic anhydrase IIneutron diffraction crystallographyNMRradiation damageXFELsX-ray crystallography

Identifiers

PMID38411550
PMCPMC10910541

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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.