ArticleJournal of synchrotron radiation2025
Advances in macromolecular crystallography at the Photon Factory: automation from crystallization to structural determination.
Article in Journal of synchrotron radiation, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- 50th anniversary of the Stanford SSRL synchrotron radiation and protein crystallography initiative.Journal of synchrotron radiation · 2026Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The Structural Biology Research Center (SBRC) and the Photon Factory at the High Energy Accelerator Research Organization (KEK) have played a key role in advancing macromolecular crystallography (MX) and have developed advanced experimental systems in the MX field. Key innovations include a long-wavelength MX beamline for native single-wavelength anomalous diffraction phasing (BL-1A), a crystal-shaping machine, an automated crystal-centering system and a fully automated diffraction data-acquisition system. In addition to the beamline technologies, the SBRC has developed a fully automated protein crystallization and monitoring system (PXS/PXS2). The crystallization plate prepared by PXS2 can be mounted directly onto an in situ data-acquisition system at BL-17A. These technologies have transformed experimental workflows, enabling high-throughput structure determination and supporting drug discovery. Furthermore, the SBRC can integrate advanced imaging techniques, including MX, cryogenic electron microscopy (cryo-EM) and small-angle X-ray scattering (SAXS), under one roof. This interdisciplinary approach facilitates hybrid structural analysis by combining techniques such as MX and SAXS or MX and cryo-EM.
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Identifiers
What OpenQuestion holds
Registered trials
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.