Evidence map›Paper›PMID 34605440›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase.

Takeshi Murakawa, Mamoru Suzuki, Toshi Arima, Michihiro Sugahara, Tomoyuki Tanaka, Rie Tanaka, So Iwata, Eriko Nango, Kensuke Tono, Hideyuki Hayashi and 4 more

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. 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
0.2field-weighted citation impact, top 54% 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, 4 citations in OpenAlex.

  1. Article
  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

14 authors at 5 institutions in 1 country.

Takeshi MurakawaDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.
Mamoru SuzukiInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Toshi ArimaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Michihiro SugaharaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Tomoyuki TanakaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Rie TanakaSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0003-1062-4792
So IwataSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Eriko NangoSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Kensuke TonoSPring-8 Center, RIKEN, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0003-1218-3759
Hideyuki HayashiDepartment of Chemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.
Kenji FukuiDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.
Takato YanoDepartment of Biochemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.
Katsuyuki TanizawaInstitute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.
Toshihide OkajimaDepartment of Chemistry, Faculty of Medicine, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan.
Osaka University of Pharmaceutical Sciences · JPKyoto University · JPSPring-8 · JPThe University of Osaka · JPTohoku University · JP

Funding

Japan Agency for Medical Research and Development JP20am0101070Japan Agency for Medical Research and Development JP21am0101070 (support number 2302)Japan Society for the Promotion of Science 19H05781Japan Society for the Promotion of Science 19K05694Japan Society for the Promotion of Science 20H05448
6 · The paper itself

Abstract

Recent advances in serial femtosecond X-ray crystallography (SFX) using X-ray free-electron lasers have paved the way for determining radiation-damage-free protein structures under nonfreezing conditions. However, the large-scale preparation of high-quality microcrystals of uniform size is a prerequisite for SFX, and this has been a barrier to its widespread application. Here, a convenient method for preparing high-quality microcrystals of a bacterial quinoprotein enzyme, copper amine oxidase from Arthrobacter globiformis, is reported. The method consists of the mechanical crushing of large crystals (5-15 mm

Indexed as

Amine Oxidase (Copper-Containing)Amino Acid SequenceArthrobacterCrystallography, X-RayLasersModels, MolecularProtein ConformationSynchrotronsTemperatureAmine Oxidase (Copper-Containing)copper amine oxidasemicrocrystalsradiation-damage-free protein structureserial femtosecond X-ray crystallographyX-ray free-electron lasers

Identifiers

PMID34605440
PMCPMC8488853
OpenAlexW3198961459

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.