EMPIAR-10752 - Single particle cryo EM Data of a human Akirin2 proteasome complex [multiple data sets in TIFF and MRC formats]

EMPIAR-10752

Single particle cryo EM Data of a human Akirin2 proteasome complex [multiple data sets in TIFF and MRC formats]

Publication:

AKIRIN2 controls the nuclear import of proteasomes in vertebrates

de Almeida M, Hinterndorfer M, Brunner H, Grishkovskaya I, Singh K, Schleiffer A, Jude J, Deswal S, Kalis R, Vunjak M, Lendl T, Imre R, Roitinger E, Neumann T, Kandolf S, Schutzbier M, Mechtler K, Versteeg GA, Haselbach D, Zuber J

Nature 599 (2021) 491-496

PMID: 34711951

DOI: 10.1038/s41586-021-04035-8

Related EMDB entry:

EMD-12341

Deposited:

2021-07-04

Released:

2021-10-01

Last modified:

2022-02-25

Imageset size:

2.16 TB

Imageset DOI:

10.6019/EMPIAR-10752

Experimental metadata:

Download xml json

Contains:

micrographs - multiframe
micrographs - single frame
picked particles - single frame - processed

Image Sets

1. Unaligned Multiframe micrographs of Akirin2 bound to the human proteasome

Category:

micrographs - multiframe

Image format:

TIFF

No. of images or tilt series:

4595

Image size:

(4092, 5760)

Pixel type:

UNSIGNED BYTE

Pixel spacing:

(1.06, 1.06)

Details:

movie files of Akirin2 recorded witha dose of 50 e-/s ona. K3 camera

Files:

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2. Motion corrected files dose weighted and summed as well as without dose weigthening

Category:

micrographs - single frame

Image format:

MRC

No. of images or tilt series:

9190

Image size:

(4092, 5760)

Pixel type:

32 BIT FLOAT

Pixel spacing:

(1.06, 1.06)

Details:

Patch motion corrected files from cryosparc

Files:

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3. Extracted particles of an Akirin2 bound proteasome

Category:

picked particles - single frame - processed

Image format:

MRC

No. of images or tilt series:

165181

Image size:

(560, 560)

Pixel type:

32 BIT FLOAT

Pixel spacing:

(1.06, 1.06)

Details:

relion extracted particle stack.

Files:

Archives and downloads the selected files into an uncompressed zip file.

We recommend using rsync, aspera, globus, etc.

Download a list of selected files.

It is possible to download files by specifying the file list with rsync command, etc.

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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)

CLEM-Reg: an automated point cloud-based registration algorithm for volume correlative light and electron microscopy.

Krentzel D, Elphick M, Domart MC, Peddie CJ, Laine RF, Shand C, Henriques R, Collinson LM, Jones ML. (2025)

CryoEMNet driven symmetry-aware molecular reconstruction through deep learning enhanced electron microscopy.

Arora S, Pan SH, Kumar S, Singh SK, Chauhan U, Alhalabi W, Arya V, Alsulami BS, Hsu CH, Chui KT, Gupta BB. (2025)

PERC: a suite of software tools for the curation of cryoEM data with application to simulation, modeling and machine learning.

Costa-Gomes B, Greer J, Juraschko N, Parkhurst J, Mirecka J, Famili M, Rangel-Smith C, Strickson O, Lowe A, Basham M, Burnley T. (2025)

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

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

Laser flash melting cryo-EM samples to overcome preferred orientation.

Straub MS, Harder OF, Mowry NJ, Barrass SV, Hruby J, Drabbels M, Lorenz UJ. (2025)

In situ structure determination of conformationally flexible targets using nextPYP.

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

EMICSS: added-value annotations for EMDB entries.

Duraisamy AK, Fonseca N, Kleywegt GJ, Patwardhan A, Morris KL. (2025)

Global conformations of <i>Pichia pastoris</i> complex I are distinguished by the binding of a unique interdomain bridging subunit.

Lee CS, Grba DN, Wright JJ, Ivanov BS, Hirst J. (2025)

Overcoming Preferred Orientation in Cryo-EM With Ultrasonic Excitation During Vitrification

Williams HM, Curtis WA, Haubner M, Hruby J, Drabbels M, Lorenz UJ. (2025)

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