Evidence map›Paper›PMID 22949190›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens.

Sarah C Atkinson, Con Dogovski, Renwick C J Dobson, Matthew A Perugini

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

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    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

4 authors at 3 institutions in 2 countries.

Sarah C AtkinsonDepartment of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria 3086, Australia.
Con Dogovski
Renwick C J Dobson
Matthew A Perugini
University of Melbourne · AULa Trobe University · AUUniversity of Canterbury · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dihydrodipicolinate synthase (DHDPS) catalyzes the first committed step of the lysine-biosynthesis pathway in bacteria, plants and some fungi. This study describes the cloning, expression, purification and crystallization of DHDPS (NP_354047.1) from the plant pathogen Agrobacterium tumefaciens (AgT-DHDPS). Enzyme-kinetics studies demonstrate that AgT-DHDPS possesses DHDPS activity in vitro. Crystals of AgT-DHDPS were grown in the unliganded form and in forms with substrate bound and with substrate plus allosteric inhibitor (lysine) bound. X-ray diffraction data sets were subsequently collected to a maximum resolution of 1.40 Å. Determination of the structure with and without substrate and inhibitor will offer insight into the design of novel pesticide agents.

Indexed as

Agrobacterium tumefaciensAmino Acid SequenceCloning, MolecularCrystallizationGene ExpressionHydro-LyasesIsoenzymesLigandsModels, MolecularMolecular Sequence DataProtein Structure, QuaternarySequence Alignment4-hydroxy-tetrahydrodipicolinate synthaseHydro-LyasesIsoenzymesLigands

Identifiers

PMID22949190
PMCPMC3433193
OpenAlexW1983472331

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.