Evidence map›Paper›PMID 29056873›Full record

ArticleCrystal growth & design2016

Characterization of Protein Nanocrystals Based on the Reversibility of Crystallization.

Katerina Dörner, Jose M Martin-Garcia, Christopher Kupitz, Zhen Gong, T Conn Mallet, Liqing Chen, Rebekka M Wachter, Petra Fromme

Abstract read
In one paragraph

Article in Crystal growth & design, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

8 authors.

Katerina DörnerSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
Jose M Martin-GarciaSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
Christopher KupitzSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
Zhen GongSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
T Conn MalletLife Science, Rigaku Americas Corporation, 9009 New Trails Drive, The Woodlands, Texas 77381, United States.
Liqing ChenSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
Rebekka M WachterSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.
Petra FrommeSchool of Molecular Sciences, Arizona State University, Box 871604, Tempe, Arizona 85287, United States.

Funding

Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
Femtosecond nano-crystallography of membrane proteinsR01GM095583 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2023
$4.3M
European Research Council 609920NIGMS NIH HHS R01 GM095583NIGMS NIH HHS U54 GM094599
6 · The paper itself

Abstract

A new approach is described to screen for protein nanocrystals based on the reversibility of crystallization. Methods to characterize nanocrystals are in strong need to facilitate sample preparation for serial femtosecond X-ray nanocrystallography (SFX). SFX enables protein structure determination by collecting X-ray diffraction from nano- and microcrystals using a free electron laser. This technique is especially valuable for challenging proteins as for example membrane proteins and is in general a powerful method to overcome the radiation damage problem and to perform time-resolved structure analysis. Nanocrystal growth cannot be monitored with common methods used in protein crystallography, as the resolution of bright field microscopy is not sufficient. A high-performance method to screen for nanocrystals is second order nonlinear imaging of chiral crystals (SONICC). However, the high cost prevents its use in every laboratory, and some protein nanocrystals may be "invisible" to SONICC. In this work using a crystallization robot and a common imaging system precipitation comprised of nanocrystals and precipitation caused by aggregated protein can be distinguished.

Identifiers

PMID29056873
PMCPMC5649632

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.