Evidence map›Paper›PMID 30224955›Full record

ArticleIUCrJ2018

S Botha, D Baitan, K E J Jungnickel, D Oberthür, C Schmidt, S Stern, M O Wiedorn, M Perbandt, H N Chapman, C Betzel

Abstract read
In one paragraph

Article in IUCrJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Article
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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.

S BothaInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
D BaitanInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
K E J JungnickelInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
D OberthürCenter for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron (DESY), Notkestrasse 85, 22607 Hamburg, Germany.
C SchmidtInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
S SternCenter for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron (DESY), Notkestrasse 85, 22607 Hamburg, Germany.
M O WiedornThe Hamburg Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.
M PerbandtInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
H N ChapmanThe Hamburg Centre for Ultrafast Imaging, Luruper Chaussee 149, 22761 Hamburg, Germany.
C BetzelInstitute of Biochemistry and Molecular Biology, Chemistry Department, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the past few years, serial crystallography methods have undergone continuous development and serial data collection has become well established at high-intensity synchrotron-radiation beamlines and XFEL radiation sources. However, the application of experimental phasing to serial crystallography data has remained a challenging task owing to the inherent inaccuracy of the diffraction data. Here, a particularly gentle method for incorporating heavy atoms into micrometre-sized crystals utilizing lipidic cubic phase (LCP) as a carrier medium is reported. Soaking in LCP prior to data collection offers a new, efficient and gentle approach for preparing heavy-atom-derivative crystals directly before diffraction data collection using serial crystallography methods. This approach supports effective phasing by utilizing a reasonably low number of diffraction patterns. Using synchrotron radiation and exploiting the anomalous scattering signal of mercury for single isomorphous replacement with anomalous scattering (SIRAS) phasing resulted in high-quality electron-density maps that were sufficient for building a complete structural model of proteinase K at 1.9 Å resolution using automatic model-building tools.

Indexed as

de novo protein structure determinationheavy-atom soakinglipidic cubic phaseserial crystallographySIRAS phasing

Identifiers

PMID30224955
PMCPMC6126645

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.