Evidence map›Paper›PMID 30511670›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

X-ray crystallographic analysis of the catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus overexpressed in Brevibacillus choshinensis.

Rattanaporn Intuy, Takafumi Itoh, Wasana Suyotha, Junji Hayashi, Shigekazu Yano, Koki Makabe, Mamoru Wakayama, Takao Hibi

Open access · greenAbstract read
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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
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

8 authors at 4 institutions in 2 countries.

Rattanaporn IntuyCollege of Life Sciences, Ritsumeikan University, Nojihigashi 1-1-1, Kusatsu, Shiga 525-8577, Japan.
Takafumi ItohDepartment of Bioscience, Fukui Prefectural University, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan.
Wasana SuyothaDepartment of Industrial Biotechnology, Prince of Songkla University, Hat Yai, Thailand.
Junji HayashiCollege of Life Sciences, Ritsumeikan University, Nojihigashi 1-1-1, Kusatsu, Shiga 525-8577, Japan.
Shigekazu YanoDepartment of Biochemical Engineering, Yamagata University, Johnan, Yonezawa, Yamagata 992-8510, Japan.
Koki MakabeDepartment of Biochemical Engineering, Yamagata University, Johnan, Yonezawa, Yamagata 992-8510, Japan.
Mamoru WakayamaCollege of Life Sciences, Ritsumeikan University, Nojihigashi 1-1-1, Kusatsu, Shiga 525-8577, Japan.ORCID 0000-0001-5027-6476
Takao HibiDepartment of Bioscience, Fukui Prefectural University, Eiheiji-cho, Yoshida-gun, Fukui 910-1195, Japan.ORCID 0000-0003-4394-4426
Ritsumeikan University · JPFukui Prefectural University · JPYamagata University · JPPrince of Songkla University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-1,3-Glucanase hydrolyzes α-1,3-glucan, an insoluble linear α-1,3-linked homopolymer of glucose that is found in the extracellular polysaccharides produced by oral streptococci in dental plaque and in fungal cell walls. This enzyme could be of application in dental care and the development of fungal cell-wall lytic enzymes, but its three-dimensional structure has not been available to date. In this study, the recombinant catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus FH11, which is classified into glycoside hydrolase family 87, was prepared using a Brevibacillus choshinensis expression system and purified in a soluble form. Crystals of the purified protein were produced by the sitting-drop vapor-diffusion method. Diffraction data were collected to a resolution of 1.6 Å using synchrotron radiation. The crystals obtained belonged to the tetragonal space group P4

Indexed as

Gene Expression Regulation, BacterialGene Expression Regulation, EnzymologicAmino Acid SequenceBrevibacillusCatalytic DomainCrystallography, X-RayGlucansGlycoside HydrolasesPaenibacillusalpha-1,3-glucanGlucansGlycoside Hydrolasescatalytic domainsPaenibacillus glycanilyticusα-1,3-glucanα-1,3-glucanase

Identifiers

PMID30511670
PMCPMC6277962
OpenAlexW2901779761

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.