Evidence map›Paper›PMID 28933304›Full record

ArticleCurrent protein & peptide science2018

Survey of Predictors of Propensity for Protein Production and Crystallization with Application to Predict Resolution of Crystal Structures.

Jianzhao Gao, Zhonghua Wu, Gang Hu, Kui Wang, Jiangning Song, Andrzej Joachimiak, Lukasz Kurgan

Abstract read
In one paragraph

Article in Current protein & peptide science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Jianzhao GaoSchool of Mathematical Sciences and LPMC, Nankai University, Tianjin, China.
Zhonghua WuSchool of Mathematical Sciences and LPMC, Nankai University, Tianjin, China.
Gang HuSchool of Mathematical Sciences and LPMC, Nankai University, Tianjin, China.
Kui WangSchool of Mathematical Sciences and LPMC, Nankai University, Tianjin, China.
Jiangning SongInfection and Immunity Program, Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Australia.
Andrzej JoachimiakMidwest Center for Structural Genomics, Argonne, IL, United States.
Lukasz KurganDepartment of Computer Science, Virginia Commonwealth University, Richmond, VA, United States.

Funding

The Midwest Center for Structural Genomics - Community ResourceR24GM115586 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2015 to 2017
$2.8M
NIGMS NIH HHS R24 GM115586
6 · The paper itself

Abstract

Selection of proper targets for the X-ray crystallography will benefit biological research community immensely. Several computational models were proposed to predict propensity of successful protein production and diffraction quality crystallization from protein sequences. We reviewed a comprehensive collection of 22 such predictors that were developed in the last decade. We found that almost all of these models are easily accessible as webservers and/or standalone software and we demonstrated that some of them are widely used by the research community. We empirically evaluated and compared the predictive performance of seven representative methods. The analysis suggests that these methods produce quite accurate propensities for the diffraction-quality crystallization. We also summarized results of the first study of the relation between these predictive propensities and the resolution of the crystallizable proteins. We found that the propensities predicted by several methods are significantly higher for proteins that have high resolution structures compared to those with the low resolution structures. Moreover, we tested a new meta-predictor, MetaXXC, which averages the propensities generated by the three most accurate predictors of the diffraction-quality crystallization. MetaXXC generates putative values of resolution that have modest levels of correlation with the experimental resolutions and it offers the lowest mean absolute error when compared to the seven considered methods. We conclude that protein sequences can be used to fairly accurately predict whether their corresponding protein structures can be solved using X-ray crystallography. Moreover, we also ascertain that sequences can be used to reasonably well predict the resolution of the resulting protein crystals.

Indexed as

Amino Acid SequenceComputational BiologyCrystallizationCrystallography, X-RayDatabases, ProteinProtein ConformationProteinsSoftwareSurveys and QuestionnairesProteinsdiffraction quality crystallizationmeta predictionpredictionprotein productionprotein structureresolution of protein crystalsX-ray crystallography

Identifiers

PMID28933304
PMCPMC7001581

What OpenQuestion holds

Textmetadata
LicenceTDM
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.