Evidence map›Paper›PMID 37747292›Full record

ArticleActa crystallographica. Section D, Structural biology2023

A user-friendly plug-and-play cyclic olefin copolymer-based microfluidic chip for room-temperature, fixed-target serial crystallography.

Zhongrui Liu, Kevin K Gu, Megan L Shelby, Deepshika Gilbile, Artem Y Lyubimov, Silvia Russi, Aina E Cohen, Sankar Raju Narayanasamy, Sabine Botha, Christopher Kupitz and 7 more

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Microfluidic Devices for High-Throughput In Situ Serial Crystallography.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Journal of applied crystallography · 2024
    Article
  8. Article
  9. Article
  10. 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

17 authors.

Zhongrui LiuDepartment of Chemical Engineering, University of California at Davis, Davis, CA 95616, USA.
Kevin K GuDepartment of Chemical Engineering, University of California at Davis, Davis, CA 95616, USA.
Megan L ShelbyBiosciences and Biotechnology Division, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA.ORCID 0000-0001-6984-957X
Deepshika GilbileDepartment of Chemical Engineering, University of California at Davis, Davis, CA 95616, USA.
Artem Y LyubimovStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Silvia RussiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.ORCID 0000-0002-9666-1465
Aina E CohenStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.ORCID 0000-0003-2414-9427
Sankar Raju NarayanasamyBiosciences and Biotechnology Division, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA.
Sabine BothaDepartment of Physics, Arizona State University, Tempe, AZ 85287, USA.
Christopher KupitzLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Raymond G SierraLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Fredric PoitevinLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Antonio GilardiLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Stella LisovaLinac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Matthew A ColemanBiosciences and Biotechnology Division, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA.
Matthias FrankBiosciences and Biotechnology Division, Lawrence Livermore National Laboratory, Livermore, CA 94550, USA.
Tonya L KuhlDepartment of Chemical Engineering, University of California at Davis, Davis, CA 95616, USA.ORCID 0000-0002-6069-0205

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
Project 1. Nanolipoprotein-supported multi-subunit vaccine for Chlamydia trachomatisU19AI144184 · NIAID · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI COLEMAN, MATTHEW ADRIAN · 2019 to 2023
$10.0M
Technology development for biological imaging with x-ray free electron lasersR01GM117342 · NIGMS · LAWRENCE LIVERMORE NATIONAL SECURITY, LLC · PI FRANK, MATTHIAS · 2016 to 2024
$4.8M
NIAID NIH HHS U19 AI144184NIGMS NIH HHS P30 GM133894NIGMS NIH HHS P30GM133894NIGMS NIH HHS R01 GM117342NIGMS NIH HHS R01GM117342
6 · The paper itself

Abstract

Over the past two decades, serial X-ray crystallography has enabled the structure determination of a wide range of proteins. With the advent of X-ray free-electron lasers (XFELs), ever-smaller crystals have yielded high-resolution diffraction and structure determination. A crucial need to continue advancement is the efficient delivery of fragile and micrometre-sized crystals to the X-ray beam intersection. This paper presents an improved design of an all-polymer microfluidic `chip' for room-temperature fixed-target serial crystallography that can be tailored to broadly meet the needs of users at either synchrotron or XFEL light sources. The chips are designed to be customized around different types of crystals and offer users a friendly, quick, convenient, ultra-low-cost and robust sample-delivery platform. Compared with the previous iteration of the chip [Gilbile et al. (2021), Lab Chip, 21, 4831-4845], the new design eliminates cleanroom fabrication. It has a larger imaging area to volume, while maintaining crystal hydration stability for both in situ crystallization or direct crystal slurry loading. Crystals of two model proteins, lysozyme and thaumatin, were used to validate the effectiveness of the design at both synchrotron (lysozyme and thaumatin) and XFEL (lysozyme only) facilities, yielding complete data sets with resolutions of 1.42, 1.48 and 1.70 Å, respectively. Overall, the improved chip design, ease of fabrication and high modifiability create a powerful, all-around sample-delivery tool that structural biologists can quickly adopt, especially in cases of limited sample volume and small, fragile crystals.

Indexed as

CycloparaffinsMuramidaseCrystallographyCrystallography, X-RayEquipment DesignMicrofluidicsPolymersProteinsTemperatureCycloparaffinsMuramidasePolymersProteinscyclic olefin copolymerfixed targetsmicrofluidicsroom-temperature SFXsample deliveryserial crystallographysynchrotronsXFELsX-ray crystallography

Identifiers

PMID37747292
PMCPMC10565732

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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.