Evidence map›Paper›PMID 28508075›Full record

ArticleScience advances2017

Fast iodide-SAD phasing for high-throughput membrane protein structure determination.

Igor Melnikov, Vitaly Polovinkin, Kirill Kovalev, Ivan Gushchin, Mikhail Shevtsov, Vitaly Shevchenko, Alexey Mishin, Alexey Alekseev, Francisco Rodriguez-Valera, Valentin Borshchevskiy and 4 more

Abstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024
    Article
  5. Review
  6. Article
  7. Single-support serial isomorphous replacement phasing.Acta crystallographica. Section D, Structural biology · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Pathways and Mechanism of Caffeine Binding to Human Adenosine AFrontiers in molecular biosciences · 2021
    Article
  14. Review
  15. Genomes of the "mSystems · 2020
    Article
  16. Article
  17. Article
  18. Review
  19. Census of halide-binding sites in protein structures.Bioinformatics (Oxford, England) · 2020
    Article
  20. 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

14 authors.

Igor MelnikovEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.
Vitaly PolovinkinInstitut de Biologie Structurale Jean-Pierre Ebel, Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, F-38000 Grenoble, France.
Kirill KovalevInstitute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.ORCID 0000-0001-5014-9602
Ivan GushchinInstitute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.ORCID 0000-0002-5348-6070
Mikhail ShevtsovMoscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia.
Vitaly ShevchenkoInstitute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.
Alexey MishinMoscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia.
Alexey AlekseevInstitute of Complex Systems (ICS), ICS-6, Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.
Francisco Rodriguez-ValeraDepartment of Vegetal Production and Microbiology, Universidad Miguel Hernández de Elche, San Juan de Alicante, Valencia, Spain.ORCID 0000-0002-9809-2059
Valentin BorshchevskiyMoscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia.
Vadim CherezovMoscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia.
Gordon A LeonardEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.
Valentin GordeliyInstitut de Biologie Structurale Jean-Pierre Ebel, Université Grenoble Alpes-Commissariat à l'Energie Atomique et aux Energies Alternatives-CNRS, F-38000 Grenoble, France.
Alexander PopovEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe a fast, easy, and potentially universal method for the de novo solution of the crystal structures of membrane proteins via iodide-single-wavelength anomalous diffraction (I-SAD). The potential universality of the method is based on a common feature of membrane proteins-the availability at the hydrophobic-hydrophilic interface of positively charged amino acid residues with which iodide strongly interacts. We demonstrate the solution using I-SAD of four crystal structures representing different classes of membrane proteins, including a human G protein-coupled receptor (GPCR), and we show that I-SAD can be applied using data collection strategies based on either standard or serial x-ray crystallography techniques.

Indexed as

IodidesScattering, Small AngleCrystallography, X-RayHumansProtein DomainsReceptors, G-Protein-CoupledIodidesReceptors, G-Protein-Coupledexperimental phasingiodideMembrane proteinSADserial crystallographyx-ray crystallography

Identifiers

PMID28508075
PMCPMC5429034

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LicenceCC BY-NC
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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.