Evidence map›Paper›PMID 41243831›Full record

ArticleActa crystallographica. Section F, Structural biology communications2025

Crystal structures of PF1765 from Pyrococcus furiosus from several different crystallization conditions with varied pH, salt and precipitant.

Sujay S Gaikwad, Beena Yadav, Shubhangi Sharma, Ashwani Kumar, Amit Kumar, Ravindra D Makde

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Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Sujay S GaikwadBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400085, India.
Beena YadavMehta Family School of Bioscience and Biomedical Engineering, Indian Institute of Technology, Indore 453552, India.
Shubhangi SharmaBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400085, India.
Ashwani KumarBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400085, India.
Amit KumarMehta Family School of Bioscience and Biomedical Engineering, Indian Institute of Technology, Indore 453552, India.
Ravindra D MakdeBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400085, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins crystallized under varied conditions typically exhibit nearly identical overall structures, with deviations confined to flexible loops or side-chain orientations. In this study, we report the extraordinary crystallization properties of PF1765 from Pyrococcus furiosus, which crystallized from the same batch of protein preparation in 104 of 192 different crystallization conditions. This yielded ten high-resolution structures (1.1-1.5 Å) across two space groups: seven in the orthorhombic space group P2

Indexed as

Archaeal ProteinsPyrococcus furiosusAmino Acid SequenceCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionHydrogen-Ion ConcentrationModels, MolecularProtein ConformationRecombinant ProteinsSaltsArchaeal ProteinsRecombinant ProteinsSaltsdifferent crystallization conditionsPF1765protein crystallographystructural conservationUPF0235

Identifiers

PMID41243831
PMCPMC12810211

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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.