Evidence map›Paper›PMID 31088963›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Unsupervised determination of protein crystal structures.

Ivan S Ufimtsev, Michael Levitt

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Solving the structure of Lgl2, a difficult blind test of unsupervised structure determination.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

2 authors.

Ivan S UfimtsevDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305 ufimtsev@stanford.edu michael.levitt@stanford.edu.ORCID 0000-0003-2632-0988
Michael LevittDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305 ufimtsev@stanford.edu michael.levitt@stanford.edu.ORCID 0000-0002-8414-7397

Funding

Emergent Properties of Complex Systems: From Atoms to Macromolecules; from Humans to SocietiesR35GM122543 · NIGMS · STANFORD UNIVERSITY · PI MICHAEL LEVITT · 2017 to 2026
$5.1M
NIGMS NIH HHS R35 GM122543
6 · The paper itself

Abstract

We present a method for automatic solution of protein crystal structures. The method proceeds with a single initial model obtained, for instance, by molecular replacement (MR). If a good-quality search model is not available, as often is the case with MR of distant homologs, our method first can automatically screen a large pool of poorly placed models and single out promising candidates for further processing if there are any. We demonstrate its utility by solving a set of synthetic cases in the 2.9- to 3.45-Å resolution.

Indexed as

Models, MolecularProteinsAlgorithmsCrystallography, X-RayProtein ConformationProteinsBcl-xLmassively parallelprotein crystal structureunsupervised method

Identifiers

PMID31088963
PMCPMC6561213

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.