Evidence map›Paper›PMID 27032894›Full record

ReviewDrug discovery today2016

Protein crystallization screens developed at the MRC Laboratory of Molecular Biology.

Fabrice Gorrec

Open access · hybridAbstract readReview
In one paragraph

Review in Drug discovery today, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Pharmaceutical science advances · 2023
    Article
  3. The FUSION protein crystallization screen.Journal of applied crystallography · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. A new soaking procedure for X-ray crystallographic structural determination of protein-peptide complexes.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Schema Matching and Data Integration with Consistent Naming on Protein Crystallization Screens.IEEE/ACM transactions on computational biology and bioinformatics
    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

1 author at 1 institution in 1 country.

Fabrice GorrecMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK. Electronic address: fgorrec@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326
6 · The paper itself

Abstract

In order to solve increasingly challenging protein structures with crystallography, crystallization reagents and screen formulations are regularly investigated. Here, we briefly describe 96-condition screens developed at the MRC Laboratory of Molecular Biology: the LMB sparse matrix screen, Pi incomplete factorial screens, the MORPHEUS grid screens and the ANGSTROM optimization screen. In this short review, we also discuss the difficulties and advantages associated with the development of protein crystallization screens.

Indexed as

CrystallizationDrug DiscoveryLaboratoriesProteinsProteins

Identifiers

PMID27032894
PMCPMC4911435
OpenAlexW2329551659

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.