Evidence map›Paper›PMID 30821703›Full record

ArticleActa crystallographica. Section D, Structural biology2019

ZOO: an automatic data-collection system for high-throughput structure analysis in protein microcrystallography.

Kunio Hirata, Keitaro Yamashita, Go Ueno, Yoshiaki Kawano, Kazuya Hasegawa, Takashi Kumasaka, Masaki Yamamoto

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing 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

93 citing papers in PubMed.

  1. Article
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  4. Crystal structure of human Dickkopf 4 cysteine-rich domain 1 and evaluation of conformational rigidity.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  5. Article
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  9. Crystal structure of PM1Pgh, a poly-γ-glutamate hydrolase from Bacillus phage PM1.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  10. Article
  11. Article
  12. Article
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  14. Enhanced capabilities for multi-crystal data collection based on double mesh scans.Acta crystallographica. Section D, Structural biology · 2025
    Article
  15. Article
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  19. Article
  20. Macromolecular crystallography at SPring-8 and SACLA.Journal of synchrotron radiation · 2025
    Article

33 more citing papers are in PubMed but not listed here.

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

7 authors.

Kunio HirataRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Keitaro YamashitaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Go UenoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Yoshiaki KawanoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.
Kazuya HasegawaJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo 679-5198, Hyogo, Japan.
Takashi KumasakaJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo 679-5198, Hyogo, Japan.ORCID 0000-0001-9289-1557
Masaki YamamotoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.ORCID 0000-0002-1311-1768

Funding

Japan Society for the Promotion of Science 15H06862
6 · The paper itself

Abstract

Owing to the development of brilliant microfocus beamlines, rapid-readout detectors and sample changers, protein microcrystallography is rapidly becoming a popular technique for accessing structural information from complex biological samples. However, the method is time-consuming and labor-intensive and requires technical expertise to obtain high-resolution protein crystal structures. At SPring-8, an automated data-collection system named ZOO has been developed. This system enables faster data collection, facilitates advanced data-collection and data-processing techniques, and permits the collection of higher quality data. In this paper, the key features of the functionality put in place on the SPring-8 microbeam beamline BL32XU are described and the major advantages of this system are outlined. The ZOO system will be a major driving force in the evolution of the macromolecular crystallography beamlines at SPring-8.

Indexed as

SoftwareAnimalsCrystallography, X-RayData CollectionHumansMuramidaseProtein ConformationProteinsReceptor, Muscarinic M2ThermolysinMuramidaseProteinsReceptor, Muscarinic M2Thermolysinautomated data collectionprotein microcrystallographyZOO

Identifiers

PMID30821703
PMCPMC6400253

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LicenceCC BY
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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.