Evidence map›Paper›PMID 19700309›Full record

ReviewCurrent opinion in structural biology2009

Recent developments in phasing and structure refinement for macromolecular crystallography.

Paul D Adams, Pavel V Afonine, Ralf W Grosse-Kunstleve, Randy J Read, Jane S Richardson, David C Richardson, Thomas C Terwilliger

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. With phases: how two wrongs can sometimes make a right.Acta crystallographica. Section D, Biological crystallography · 2010
    Article
  15. PHENIX: a comprehensive Python-based system for macromolecular structure solution.Acta crystallographica. Section D, Biological crystallography · 2010
    Article
  16. MolProbity: all-atom structure validation for macromolecular crystallography.Acta crystallographica. Section D, Biological crystallography · 2010
    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.

Paul D AdamsLawrence Berkeley National Laboratory, BLDG 64R0121, 1 Cyclotron Road, Berkeley, CA 94720, USA. PDAdams@lbl.gov
Pavel V Afonine
Ralf W Grosse-Kunstleve
Randy J Read
Jane S Richardson
David C Richardson
Thomas C Terwilliger

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
NIGMS NIH HHS 1P01 GM063210NIGMS NIH HHS P01 GM063210Wellcome Trust 082961
6 · The paper itself

Abstract

Central to crystallographic structure solution is obtaining accurate phases in order to build a molecular model, ultimately followed by refinement of that model to optimize its fit to the experimental diffraction data and prior chemical knowledge. Recent advances in phasing and model refinement and validation algorithms make it possible to arrive at better electron density maps and more accurate models.

Indexed as

Crystallography, X-RayHumansImaging, Three-DimensionalMacromolecular SubstancesModels, MolecularMacromolecular Substances

Identifiers

PMID19700309
PMCPMC2763973

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.