REL
2017-04-09
2018-07-18
2018-07-18
Nucleotide-Driven Triple-State Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome
0000-0001-9302-2257
Youdong
Jack
Mao
Dana-Farber Cancer Institute
450 Brookline Ave
Boston
MA
United States
02215
0000-0001-9302-2257
Youdong
Jack
Mao
Dana-Farber Cancer Institute
450 Brookline Ave
Boston
MA
United States
02215
Zhu Y
Wang WL
Mao Y
2.8
10.6019/EMPIAR-10090
EMDB
EMD-8662
EMD-8663
EMD-8664
EMD-8665
EMD-8666
EMD-8667
EMD-8668
Zhu Y
Wang WL
Yu D
Ouyang Q
Lu Y
Mao Y
Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome
Nature communications
Nat Commun
United States
1
9
2018
English
10.1038/s41467-018-03785-w
29636472
Motion-corrected single frame micrographs of ATP-gS-bound human proteasome
/data/micrographs
micrographs - single frame
MRC
MRC
8463
1
32 BIT FLOAT
7420
0.75
7676
0.75
Each micrograph is averaged from drift-corrected 30 frames with an accumulated dose of 30 electrons/anstrom^2.
Single-particle stacks of classified conformations
/data
picked particles - multiframe - processed
MRCS
MRCS
502384
1
32 BIT FLOAT
560
0.75
560
0.75
The single-particle datasets have been classified into six classes: SA, SB, SC, SD1, SD2, SD3. The SD20S is a combined data set of SD1, SD2 and SD3 to focus refinement on the 20S CP component of the human proteasome in an open-gate state.