Crystallization of Microbial Rhodopsins.

Kirill Kovalev, Roman Astashkin, Valentin Gordeliy, Vadim Cherezov

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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

1.9field-weighted citation impact, top 14% of its field

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.

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3 · Its place in the literature

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1 citing paper in PubMed, 3 citations in OpenAlex.

Custom Design of a Humidifier Chamber forCrystal growth & design · 2024
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4 · The record

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5 · Who and what money

Authors and funding

4 authors at 4 institutions in 4 countries.

Kirill KovalevInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Roman AstashkinInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Valentin GordeliyInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CEA, CNRS, Grenoble, France.

Vadim CherezovBridge Institute, Department of Chemistry, University of Southern California, Los Angeles, CA, USA. cherezov@usc.edu.

Institut de Biologie Structurale · FRRWTH Aachen University · DEUniversité Grenoble Alpes · FRUniversity of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial rhodopsins are light-sensitive transmembrane proteins, evolutionary adapted by various organisms like archaea, bacteria, simple eukaryote, and viruses to utilize solar energy for their survival. A complete understanding of functional mechanisms of these proteins is not possible without the knowledge of their high-resolution structures, which can be primarily obtained by X-ray crystallography. This technique, however, requires high-quality crystals, growing of which is a great challenge especially in case of membrane proteins. In this chapter, we summarize methods applied for crystallization of microbial rhodopsins with the emphasis on crystallization in lipidic mesophases, also known as in meso approach. In particular, we describe in detail the methods of crystallization using lipidic cubic phase to grow both large crystals optimized for traditional crystallographic data collection and microcrystals for serial crystallography.

Indexed as

Membrane ProteinsRhodopsins, MicrobialCrystallizationCrystallography, X-RayLipidsLipidsMembrane ProteinsRhodopsins, MicrobialBicellesCrystallizationIn mesoLipidic cubic phaseMembrane fusionMicrobial rhodopsinsSerial crystallographyX-ray diffraction

Identifiers

PMID35857226

DOI10.1038/nprot.2014.141

OpenAlexW4286355514

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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.