Evidence map›Paper›PMID 42244436›Full record

ArticleFEBS open bio2026

Refinement of amino-acid conformation vs. difference density maps in time-resolved serial femtosecond crystallography data analysis.

Meng Iao Fong, Yuhei Hosokawa, Lars Oliver Essen, Manuel Maestre-Reyna

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

4 authors.

Meng Iao FongDepartment of Chemistry, National Taiwan University, Taipei, Taiwan.
Yuhei HosokawaDepartment of Chemistry, National Taiwan University, Taipei, Taiwan.ORCID https://orcid.org/0000-0001-9559-8567
Lars Oliver EssenDepartment of Chemistry, Philipps University Marburg, Germany.
Manuel Maestre-ReynaDepartment of Chemistry, National Taiwan University, Taipei, Taiwan.ORCID https://orcid.org/0000-0002-9566-7216

Funding

National Science and Technology Council 111-2113-M-002-029-MY3National Science and Technology Council 113-2123-M-002 -013National Science and Technology Council 113-2811-M-002-033-MY2National Science and Technology Council 114-2628-M-002 -010 -MY4National Taiwan University 112 L8943
6 · The paper itself

Abstract

Time-resolved crystallography is a revolutionary X-ray diffraction technique by which the structural features of short-lived, transient intermediates of in crystallo reactions can be elucidated. While visualizing time-dependent structural changes via difference electron density maps is relatively simple, time-resolved diffraction data is complex because it arises from a substrate-dominated mix of the different reaction components. Thus, atomic coordinate refinement of intermediate species is challenging and prone to bias, as it requires deconvolution of the mixed-states. To simplify the refinement process, we have developed difference electron density correlation coefficient real space refinement (dFoCC refinement). By basing coordinate refinement on comparing observed vs. calculated difference density maps, dFoCC produces reasonable atomic coordinates of intermediate species in a reproducible manner and with clearly defined quality metrics.

Indexed as

Amino AcidsCrystallography, X-RayData AnalysisProtein ConformationAmino Acidscoordinate refinementdifference density mapstructural biologytime‐resolved crystallography

Identifiers

PMID42244436
PMCPMC13398853

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.