Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip

Dunce J, Salmon L, Davies O, Communications Biology 5(1) (2022) DOI

SASDNS5 – Meiosis protein TEX12 (Testis-expressed protein 12) – F109E mutant

Testis-expressed protein 12 (F109E)
MWexperimental 21 kDa
MWexpected 18 kDa
VPorod 30 nm3
log I(s) 4.17×10-3 4.17×10-4 4.17×10-5 4.17×10-6
Testis-expressed protein 12 (F109E) small angle scattering data  s, nm-1
ln I(s)
Testis-expressed protein 12 (F109E) Guinier plot ln 4.17×10-3 Rg: 2.3 nm 0 (2.3 nm)-2 s2
Testis-expressed protein 12 (F109E) Kratky plot 1.104 0 3 sRg
Testis-expressed protein 12 (F109E) pair distance distribution function Rg: 2.3 nm 0 Dmax: 7.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Testis-expressed protein 12 (F109E) DAMMIF model
Testis-expressed protein 12 (F109E) DAMFILT model

log I(s)
 s, nm-1
Testis-expressed protein 12 (F109E) ROSETTA model

Synchrotron SAXS data from solutions of the meiosis protein TEX12 (α-helical core, single mutant) in 20 mM Tris, 150 mM KCl, pH 8 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.095 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 10 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column. 20 successive 3 second frames were collected through the sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Testis-expressed protein 12 (F109E) (TEX12 - F mutant)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   9.1 kDa
UniProt   Q9BXU0 (49-123)
Sequence   FASTA