Evidence map›Paper›PMID 8520493›Full record

ArticleProtein science : a publication of the Protein Society1995

Crystallization and preliminary X-ray analysis of electron transfer flavoproteins from human and Paracoccus denitrificans.

D L Roberts, K R Herrick, F E Frerman, J J Kim

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1995. 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
0.7field-weighted citation impact, top 30% 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, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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 2 institutions in 1 country.

D L RobertsDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee 53226, USA.
K R Herrick
F E Frerman
J J Kim
Medical College of Wisconsin · USUniversity of Colorado Health · US

Funding

STRUCTURE /FUNCTION OF A FLAVOPROTEIN DEHYDROGENASER01GM029076 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI KIM, JUNG JA P. · 1985 to 2015
$4.4M
ELECTRON TRANSFER FLAVOPROTEIN AND GLUTARIC ACIDEMIA IIR01DK049726 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI FRERMAN, FRANK E · 1995 to 1998
–
NICHD NIH HHS HD07385NIDDK NIH HHS DK49726NIGMS NIH HHS GM29076
6 · The paper itself

Abstract

Mammalian electron transfer flavoprotein (ETF) is a soluble, heterodimeric flavoprotein responsible for the oxidation of at least nine primary matrix flavoprotein dehydrogenases. Crystals have been obtained for the recombinant human electron transfer flavoprotein (ETFhum) by the sitting-drop vapor diffusion technique using polyethylene glycol (PEG) 1500 at pH 7.0 as the precipitating agent. ETFhum crystallizes in the monoclinic space group P2(1), with unit cell parameters a = 47.46 angstrum, b = 104.10 angstrum, c = 63.79 angstrum, and beta = 110.02 degrees. Based on the assumption of one alpha beta dimer per asymmetric unit, the Vm value is 2.69 angstrum 3/Da. A native data set has been collected to 2.1 angstrum resolution. One heavy-atom derivative has also been obtained by soaking a preformed crystal of ETFhum in 2 mM thimerosal solution for 2h at 19 degrees C. Patterson analysis indicates one major site. The analogous electron transfer flavoprotein from Paracoccus denitrificans (ETFpar) has also been crystallized using PEG 8000 at pH 5.5 as the precipitating agent. ETFpar crystallizes in the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 79.98 angstrum, b = 182.90 angstrum, and c = 70.07 angstrum. The Vm value of 2.33 angstrum 3/Da is consistent with two alpha beta dimers per asymmetric unit. A native data set has been collected to 2.5 angstrum resolution.

Indexed as

Bacterial ProteinsCrystallizationCrystallography, X-RayElectron-Transferring FlavoproteinsElectron TransportFlavoproteinsHumansParacoccusBacterial ProteinsElectron-Transferring FlavoproteinsFlavoproteins

Identifiers

PMID8520493
PMCPMC2143193
OpenAlexW2137639214

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.