» Articles » PMID: 10600557

Haloarcula Marismortui 50S Subunit-complementarity of Electron Microscopy and X-Ray Crystallographic Information

Overview
Journal J Struct Biol
Date 1999 Dec 22
PMID 10600557
Citations 5
Authors
Affiliations
Soon will be listed here.
Abstract

The large 50S subunit of the Haloarcula marismortui 70S ribosome was solved to 19 A using cryo-electron microscopy and single particle reconstruction techniques and to 9 A using X-ray crystallography. In the latter case, phases were determined by multiple isomorphous replacement and anomalous scattering from three heavy atom derivatives. The availability of X-ray and electron microscopy (EM) data has made it possible to compare the results of the two experimental methods. In the flexible regions of the 50S subunit, small differences in the mass distribution were detected. These differences can be attributed to the influence of packing in the crystal cell. The rotationally averaged power spectra of X-ray and EM were compared in an overlapping spatial frequency range from 60 to 13 A. The resulting ratio of X-ray to EM power ranges from 1 to 15, reflecting a progressively larger underestimation of the Fourier amplitudes by the electron microscope.

Citing Articles

Net Charges of the Ribosomal Proteins of the and Clusters of Halophiles Are Inversely Related to the Degree of Halotolerance.

Tirumalai M, Anane-Bediakoh D, Rajesh S, Fox G Microbiol Spectr. 2021; 9(3):e0178221.

PMID: 34908470 PMC: 8672879. DOI: 10.1128/spectrum.01782-21.


Cryo-electron microscopy visualization of a large insertion in the 5S ribosomal RNA of the extremely halophilic archaeon Halococcus morrhuae.

Tirumalai M, Kaelber J, Park D, Tran Q, Fox G FEBS Open Bio. 2020; 10(10):1938-1946.

PMID: 32865340 PMC: 7530397. DOI: 10.1002/2211-5463.12962.


Structure of the TRPA1 ion channel suggests regulatory mechanisms.

Paulsen C, Armache J, Gao Y, Cheng Y, Julius D Nature. 2015; 520(7548):511-7.

PMID: 25855297 PMC: 4409540. DOI: 10.1038/nature14367.


Mechanistic insights into the recycling machine of the SNARE complex.

Zhao M, Wu S, Zhou Q, Vivona S, Cipriano D, Cheng Y Nature. 2015; 518(7537):61-7.

PMID: 25581794 PMC: 4320033. DOI: 10.1038/nature14148.


Fabs enable single particle cryoEM studies of small proteins.

Wu S, Avila-Sakar A, Kim J, Booth D, Greenberg C, Rossi A Structure. 2012; 20(4):582-92.

PMID: 22483106 PMC: 3322386. DOI: 10.1016/j.str.2012.02.017.