Structural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations

Jana Aupič.

SASDXJ3 – Human major vault protein

Major vault protein
MWexperimental 7660 kDa
MWexpected 7747 kDa
VPorod 16650 nm3
log I(s) 3.95×102 3.95×101 3.95×100 3.95×10-1
Major vault protein small angle scattering data  s, nm-1
ln I(s)
Major vault protein Guinier plot ln 3.95×102 Rg: 16.3 nm 0 (16.3 nm)-2 s2
(sRg)2I(s)/I(0)
Major vault protein Kratky plot 1.104 0 √3 sRg
p(r)
Major vault protein pair distance distribution function Rg: 22.4 nm 0 Dmax: 65 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Major vault protein OTHER [STATIC IMAGE] model
log I(s)
 s, nm-1
Major vault protein OTHER [STATIC IMAGE] model
log I(s)
 s, nm-1
Major vault protein OTHER [STATIC IMAGE] model
Synchrotron SAXS data from solutions of human major vault protein in 25 mM HEPES, 150 mM NaCl, 1 mM TCEP, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Two samples at a concentration of 0.5 mg/mL were measured at 20°C. For each sample measurement, ten X-ray scattering measurements with 1-second exposure times were collected. The data were normalized to the intensity of the transmitted beam and radially averaged. Ten analogous sample frames were averaged, and buffer scattering was subtracted from the sample data.

All samples were centrifuged at 20,000 × g for 10 min at 4°C prior analysis. Guinier analysis cannot be reliable performed due to the size of the particle. The atomic coordinate files of the models displayed in this entry are made available in the 'Additional files' folder of the full entry zip archive.

Major vault protein (MVP)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Other
Mon. MW   99.3 kDa
 
UniProt   Q14764 (1-893)
Sequence   FASTA