Evidence map›Paper›PMID 19255476›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009

Crystallization and preliminary X-ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate.

Sarah C Atkinson, Renwick C J Dobson, Janet M Newman, Michael A Gorman, Con Dogovski, Michael W Parker, Matthew A Perugini

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  4. Article
  5. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the grapevine Vitis vinifera.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  6. Crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  7. Crystallization and preliminary X-ray diffraction analysis of L,L-diaminopimelate aminotransferase (DapL) from Chlamydomonas reinhardtii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  8. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  9. Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  10. Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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

7 authors at 3 institutions in 1 country.

Sarah C AtkinsonDepartment of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria, Australia.
Renwick C J Dobson
Janet M Newman
Michael A Gorman
Con Dogovski
Michael W Parker
Matthew A Perugini
University of Melbourne · AUSt Vincents Institute of Medical Research · AUCommonwealth Scientific and Industrial Research Organisation · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this paper, the crystallization and preliminary X-ray diffraction analysis to near-atomic resolution of DHDPS from Clostridium botulinum crystallized in the presence of its substrate pyruvate are presented. The enzyme crystallized in a number of forms using a variety of PEG precipitants, with the best crystal diffracting to 1.2 A resolution and belonging to space group C2, in contrast to the unbound form, which had trigonal symmetry. The unit-cell parameters were a = 143.4, b = 54.8, c = 94.3 A, beta = 126.3 degrees . The crystal volume per protein weight (V(M)) was 2.3 A(3) Da(-1) (based on the presence of two monomers in the asymmetric unit), with an estimated solvent content of 46%. The high-resolution structure of the pyruvate-bound form of C. botulinum DHDPS will provide insight into the function and stability of this essential bacterial enzyme.

Indexed as

Clostridium botulinumCrystallizationCrystallography, X-RayHydro-LyasesPyruvic AcidRecombinant ProteinsSubstrate Specificity4-hydroxy-tetrahydrodipicolinate synthaseHydro-LyasesPyruvic AcidRecombinant Proteins

Identifiers

PMID19255476
PMCPMC2650466
OpenAlexW2008407101

What OpenQuestion holds

Textmetadata
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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.