Evidence map›Paper›PMID 41959872›Full record

ArticleJournal of applied crystallography2026

A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons.

Swagatha Ghosh, Analia Banacore, Per Norder, Monica Bjelčić, Arpitha Kabbinale, Padmini Nileshwar, Gabrielle Wehlander, Daniele de Sanctis, Shibom Basu, Julien Orlans and 4 more

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Swagatha GhoshDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0003-1063-0674
Analia BanacoreDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0002-2630-8797
Per NorderDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.
Monica BjelčićBioMAX Beamline, MAX IV Laboratory Lund University Sweden.ORCID https://orcid.org/0000-0001-5020-0252
Arpitha KabbinaleDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0002-7031-7703
Padmini NileshwarDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.
Gabrielle WehlanderDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0001-8135-0202
Daniele de SanctisEuropean Synchrotron Radiation Facility Grenoble France.ORCID https://orcid.org/0000-0003-0391-8290
Shibom BasuEuropean Molecular Biology Laboratory, Grenoble, France.ORCID https://orcid.org/0000-0001-6484-8236
Julien OrlansEuropean Synchrotron Radiation Facility Grenoble France.ORCID https://orcid.org/0000-0002-6933-2287
Adams VallejosDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0001-6531-2118
Leonard M G ChavasDepartment of Applied Physics, Graduate School of Engineering Nagoya University Japan.ORCID https://orcid.org/0000-0001-9973-9355
Richard NeutzeDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.ORCID https://orcid.org/0000-0003-0986-6153
Gisela BrändénDepartment of Chemistry and Molecular Biology Gothenburg University Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fixed-target platforms provide convenient support for microcrystals during serial X-ray crystallography studies using synchrotron radiation. Here, we describe a simple user-friendly 3D-printed support where the crystals are sandwiched between two layers of thin X-ray-transparent membrane resulting in very low scattering background. The platform is compatible with magnetic mounting onto the standard goniometer of macromolecular crystallography beamlines. Our design utilizes a 96-well frame that facilitates hanging-drop experiments directly on the membrane using conventional crystallization plates, thereby eliminating multiple pipetting and crystal handling steps. Crystals can be enclosed in a sandwich and packed into 'cassettes', preventing the risk of the sample drying out during room-temperature transportation to synchrotron sources. The versatility of the platform is demonstrated by five structures solved using different crystallization and data-collection strategies. Lysozyme single-crystal rotational crystallography at room temperature is shown, as well as microcrystal serial data collection under cryogenic conditions. On-chip microcrystallization is illustrated by use of a photosynthetic reaction center as an example. Finally, serial crystallography data collection at room temperature from microcrystals of the membrane protein cytochrome

Indexed as

fixed-target chipsin situ crystallizationmacromolecular crystallographyroom-temperature protein structuresserial synchrotron X-ray crystallography

Identifiers

PMID41959872
PMCPMC13060402

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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.