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2024-06-03
2025-03-20
2025-03-20
Single-particle cryo-EM structure of the RNA chaperone Hfq in a translation repression complex Hfq-Crc-estA
0000-0003-1144-9877
Bonaventura
Luisi
Department of Biochemistry, Sanger Building, University of Cambridge
80 Tennis Court Road
Cambridge
Cambridgeshire
United Kingdom
CB2 1GA
0000-0003-1144-9877
Bonaventura
Luisi
Department of Biochemistry, Sanger Building, University of Cambridge
80 Tennis Court Road
Cambridge
Cambridgeshire
United Kingdom
CB2 1GA
Dendooven T
Sonnleitner E
Bläsi U
Luisi BF
Wellcome Trust
200873/Z/16/Z
United Kingdom
4.3
10.6019/EMPIAR-12206
EMDB
molecule
EMD-16265
Dendooven T
Sonnleitner E
Bläsi U
Luisi BF
Translational regulation by Hfq-Crc assemblies emerges from polymorphic ribonucleoprotein folding
The EMBO journal
EMBO J
United Kingdom
3
42
2022
English
10.15252/embj.2022111129
36504222
Unaligned micrographs of the Hfq-Crc-estA translation repression complex.
Multiframe micrographs of the Hfq-Crc translation repression complex formed on estA(118)
/data/Hfq-Crc-estA
micrographs - multiframe
TIFF
TIFF
13651
47
UNSIGNED BYTE
11520
0.83
8184
0.83
Hfq/Crc translation repression complex formed on estA(118) present in micrographs. The images were taken using an FEI Titan Krios G2, 300kV, with an average electron dose per frame of 1.02 electrons per square Angstrom. Defocus -1.1 to -2.5um.