Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes.

Daccache D, De Jonge E, Liloku P, Mechleb K, Haddad M, Corthaut S, Sterckx YG, Volkov AN, Claeys Bouuaert C, Genes Dev 37(11-12):535-553 (2023) Europe PMC

SASDSR2 – Zea mays PAIR1 coiled-coiled with N-terminal SUMO-tag

Protein PAIR1
MWexperimental 130 kDa
MWexpected 132 kDa
log I(s) 6.75×10-2 6.75×10-3 6.75×10-4 6.75×10-5
Protein PAIR1 small angle scattering data  s, nm-1
ln I(s)
Protein PAIR1 Guinier plot ln 6.76×10-2 Rg: 8.0 nm 0 (8.0 nm)-2 s2
(sRg)2I(s)/I(0)
Protein PAIR1 Kratky plot 1.104 0 √3 sRg
p(r)
Protein PAIR1 pair distance distribution function Rg: 8.8 nm 0 Dmax: 31.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
Protein PAIR1 OTHER model
log I(s)
 s, nm-1
Synchrotron SAXS data from solutions of Zea mays PAIR1 coiled-coiled with N-terminal SUMO-tag in 25 mM HEPES-NaOH, 500 mM NaCl, 5 mM EDTA, 5% glycerol, 1 mM DTT, pH 7.5 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.099 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 90.00 μl sample at 13.4 mg/ml was injected at a 0.20 ml/min flow rate onto a Shodex KW404-4F column at 15°C. 960 successive 0.990 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Protein PAIR1 (PAIR1)
Mol. type   Protein
Organism   Zea mays
Olig. state   Tetramer
Mon. MW   33.0 kDa
 
UniProt   A0A804LC01 (30-200)
Sequence   FASTA