Evidence map›Paper›PMID 29952383›Full record

ArticleLab on a chip2018

Crystal-on-crystal chips for in situ serial diffraction at room temperature.

Zhong Ren, Medine Ayhan, Sepalika Bandara, Kalinga Bowatte, Indika Kumarapperuma, Semini Gunawardana, Heewhan Shin, Cong Wang, Xiaoli Zeng, Xiaojing Yang

Abstract read
In one paragraph

Article in Lab on a chip, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Microfluidic Devices for High-Throughput In Situ Serial Crystallography.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. A standard descriptor for fixed-target serial crystallography.Acta crystallographica. Section D, Structural biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Crystal structure of a far-red-sensing cyanobacteriochrome reveals an atypical bilin conformation and spectral tuning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

10 authors.

Zhong RenDepartment of Chemistry, The University of Illinois at Chicago, Chicago, IL 60607, USA. zren@uic.edu xiaojing@uic.edu.
Medine Ayhan
Sepalika Bandara
Kalinga Bowatte
Indika Kumarapperuma
Semini Gunawardana
Heewhan Shin
Cong Wang
Xiaoli Zeng
Xiaojing Yang

Funding

Structures, Dynamics and Signaling Mechanisms of Modular PhotoreceptorsR01EY024363 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YANG, XIAOJING · 2014 to 2021
$2.9M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
NEI NIH HHS R01 EY024363NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

Recent developments in serial crystallography at X-ray free electron lasers (XFELs) and synchrotrons have been driven by two scientific goals in structural biology - first, static structure determination from nano or microcrystals of membrane proteins and large complexes that are difficult for conventional cryocrystallography, and second, direct observations of transient structural species in biochemical reactions at near atomic resolution. Since room-temperature diffraction experiments naturally demand a large quantity of purified protein, sample economy is critically important for all steps of serial crystallography from crystallization, crystal delivery to data collection. Here we report the development and applications of "crystal-on-crystal" devices to facilitate large-scale in situ serial diffraction experiments on protein crystals of all sizes - large, small, or microscopic. We show that the monocrystalline quartz as a substrate material prevents vapor loss during crystallization and significantly reduces background X-ray scattering. These devices can be readily adopted at XFEL and synchrotron beamlines, which enable efficient delivery of hundreds to millions of crystals to the X-ray beam, with an overall protein consumption per dataset comparable to that of cryocrystallography.

Indexed as

TemperatureCrystallography, X-RayEquipment DesignSynchrotrons

Identifiers

PMID29952383
PMCPMC6057835

What OpenQuestion holds

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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.