Evidence map›Paper›PMID 38846758›Full record

ArticleJournal of applied crystallography2024

Dennis E Brookner, Doeke R Hekstra

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024
    Review
  6. Journal of applied crystallography · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Dennis E BrooknerDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, USA.ORCID https://orcid.org/0000-0003-2827-4743
Doeke R HekstraDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, USA.ORCID https://orcid.org/0000-0003-2332-9223

Funding

Identifying Principles of Protein Mechanics by Applying Force and Observing MotionDP2GM141000 · NIGMS · HARVARD UNIVERSITY · PI HEKSTRA, DOEKE ROMKE · 2020 to 2020
$2.4M
NIGMS NIH HHS DP2 GM141000
6 · The paper itself

Abstract

Conformational change mediates the biological functions of macromolecules. Crystallographic measurements can map these changes with extraordinary sensitivity as a function of mutations, ligands and time. A popular method for detecting structural differences between crystallographic data sets is the isomorphous difference map. These maps combine the phases of a chosen reference state with the observed changes in structure factor amplitudes to yield a map of changes in electron density. Such maps are much more sensitive to conformational change than structure refinement is, and are unbiased in the sense that observed differences do not depend on refinement of the perturbed state. However, even modest changes in unit-cell properties can render isomorphous difference maps useless. This is unnecessary. Described here is a generalized procedure for calculating observed difference maps that retains the high sensitivity to conformational change and avoids structure refinement of the perturbed state. This procedure is implemented in an open-source Python package,

Indexed as

difference mapsopen-source softwareX-ray crystallography

Identifiers

PMID38846758
PMCPMC11151677

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.