EMPIAR-11581 - Cryo electron microscopy micrographs of high molecular weight fractions from yeast native cell extracts [51497 multi-frame micrographs composed of 972 frames each in EER format]

EMPIAR-11581

Cryo electron microscopy micrographs of high molecular weight fractions from yeast native cell extracts [51497 multi-frame micrographs composed of 972 frames each in EER format]

Publication:

Delineating organizational principles of the endogenous L-A virus by cryo-EM and computational analysis of native cell extracts

Schmidt L, Tüting C, Kyrilis FL, Hamdi F, Semchonok DA, Hause G, Meister A, Ihling C, Stubbs MT, Sinz A, Kastritis PL

Communications biology 7 (2024)

PMID: 38730276

DOI: 10.1038/s42003-024-06204-7

Related EMDB entry:

EMD-17628

Deposited:

2022-12-13

Released:

2024-05-29

Last modified:

2024-06-17

Imageset size:

26.22 TB

Imageset DOI:

10.6019/EMPIAR-11581

Experimental metadata:

Download xml json

Contains:

micrographs - multiframe

Image Sets

1. unaligned multi-frame micrographs of a high-molecular yeast fraction

Category:

micrographs - multiframe

Image format:

EER

No. of images or tilt series:

51497

Image size:

(4096, 4096)

Pixel type:

BIT

Pixel spacing:

(0.93, 0.93)

Details:

This dataset provides the cryo-electron microscopy (cryo-EM) analysis of high molecular weight biomolecules isolated from Saccharomyces cerevisiae, commonly known as baker's yeast. The cells were grown, lysed, and the lysate was subsequently cleared and fractionated using size exclusion chromatography. The data focuses on fraction #5, known for its rich composition of ribosomes and L-A virus capsids. The cryo-EM data presented here offers a comprehensive visualization of these essential biomolecular structures, providing an insightful perspective into their structural organization and potentially informing future studies of yeast cellular processes and viral interactions.

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Citations

High-resolution ab initio reconstruction enables cryo-EM structure determination of small particles

Kim K, Li H, Clarke OB. (2025)

Self-supervised learning for generalizable particle picking in cryo-EM micrographs.

Zamanos A, Koromilas P, Bouritsas G, Kastritis PL, Panagakis Y. (2025)

In situ structure determination of conformationally flexible targets using nextPYP.

Liu HF, Zhou Y, Huang Q, Martin J, Bartesaghi A. (2025)

CryoPROS: Correcting misalignment caused by preferred orientation using AI-generated auxiliary particles.

Zhang H, Zheng D, Wu Q, Yan N, Peng H, Hu Q, Peng Y, Yan Z, Shi Z, Bao C, Hu M. (2025)

Few-shot learning for non-vitrified ice segmentation.

Vivas-Lago A, Castaño-Díez D. (2025)

Automated removal of corrupted tilts in cryo-electron tomography.

Majtner T, Turoňová B. (2025)

Reanalysis of cryo-EM data reveals ALK-cytokine assemblies with both 2:1 and 2:2 stoichiometries.

Felix J, De Munck S, Bazan JF, Savvides SN. (2025)

Probabilistic single-particle cryo-EM ab initio 3D reconstruction in SIMPLE.

Van CTS, Reboul CF, Caesar JJE, Meana-Pañeda R, Lountos GT, Deme JC, Bryant OJ, Johnson S, Piczak CT, Valkov E, Lea SM, Elmlund H. (2025)

Cryo-EM Structure Reconstruction by Gaussian Splatting: Pushing the Resolution to Extreme

Zeng B, Liu S, Cheng S, Xu G, Fan H. (2025)

Molecular exaptation by the integrin αI domain.

Hollis JA, Chan MC, Malik HS, Campbell MG. (2025)

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