Evidence map›Paper›PMID 21359836›Full record

ArticleJournal of structural and functional genomics2011

SAD phasing using iodide ions in a high-throughput structural genomics environment.

Jan Abendroth, Anna S Gardberg, John I Robinson, Jeff S Christensen, Bart L Staker, Peter J Myler, Lance J Stewart, Thomas E Edwards

Abstract read
In one paragraph

Article in Journal of structural and functional genomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

52 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Structural and biochemical characterization ofProcess biochemistry (Barking, London, England) · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Census of halide-binding sites in protein structures.Bioinformatics (Oxford, England) · 2020
    Article
  9. Structural diversity in the Mycobacteria DUF3349 superfamily.Protein science : a publication of the Protein Society · 2020
    Article
  10. Toward a structome of Acinetobacter baumannii drug targets.Protein science : a publication of the Protein Society · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  17. Article
  18. Structure of acid deoxyribonuclease.Nucleic acids research · 2017
    Article
  19. 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

8 authors.

Jan AbendrothEmerald BioStructures, 7869 NE Day Road West, Bainbridge Island, WA 98110, USA.
Anna S Gardberg
John I Robinson
Jeff S Christensen
Bart L Staker
Peter J Myler
Lance J Stewart
Thomas E Edwards

Funding

NIAID NIH HHS HHSN272200700057C
6 · The paper itself

Abstract

The Seattle Structural Genomics Center for Infectious Disease (SSGCID) focuses on the structure elucidation of potential drug targets from class A, B, and C infectious disease organisms. Many SSGCID targets are selected because they have homologs in other organisms that are validated drug targets with known structures. Thus, many SSGCID targets are expected to be solved by molecular replacement (MR), and reflective of this, all proteins are expressed in native form. However, many community request targets do not have homologs with known structures and not all internally selected targets readily solve by MR, necessitating experimental phase determination. We have adopted the use of iodide ion soaks and single wavelength anomalous dispersion (SAD) experiments as our primary method for de novo phasing. This method uses existing native crystals and in house data collection, resulting in rapid, low cost structure determination. Iodide ions are non-toxic and soluble at molar concentrations, facilitating binding at numerous hydrophobic or positively charged sites. We have used this technique across a wide range of crystallization conditions with successful structure determination in 16 of 17 cases within the first year of use (94% success rate). Here we present a general overview of this method as well as several examples including SAD phasing of proteins with novel folds and the combined use of SAD and MR for targets with weak MR solutions. These cases highlight the straightforward and powerful method of iodide ion SAD phasing in a high-throughput structural genomics environment.

Indexed as

Amino Acid SequenceBabesia bovisBacterial ProteinsBinding SitesCloning, MolecularCoccidioidesCrystallography, X-RayFructose-Bisphosphate AldolaseIodidesModels, MolecularMolecular Sequence DataMycobacterium aviumPhosphoric Monoester HydrolasesProtein Structure, SecondaryProtozoan ProteinsSequence AlignmentBacterial ProteinsFructose-Bisphosphate AldolaseIodidesPhosphoric Monoester Hydrolasesphosphoserine phosphataseProtozoan Proteins

Identifiers

PMID21359836
PMCPMC3123459

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LicenceCC BY-NC
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Registered trials

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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.