Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.

Xi Z, Whitley MJ, Gronenborn AM, Structure 25(3):496-505 (2017) Europe PMC

SASDBT9 – Full-length human βB2-crystallin

Beta-crystallin B2
MWexperimental 42 kDa
MWexpected 46 kDa
VPorod 67 nm3
log I(s) 7.40×10-2 7.40×10-3 7.40×10-4 7.40×10-5
Beta-crystallin B2 small angle scattering data  s, nm-1
ln I(s)
Beta-crystallin B2 Guinier plot ln 7.40×10-2 Rg: 2.2 nm 0 (2.2 nm)-2 s2
(sRg)2I(s)/I(0)
Beta-crystallin B2 Kratky plot 1.104 0 √3 sRg
p(r)
Beta-crystallin B2 pair distance distribution function Rg: 2.3 nm 0 Dmax: 8.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Beta-crystallin B2 DAMMIN model
Synchrotron SAXS data from solutions of full-length human βB2-crystallin in 25 mM sodium phosphate, 5 mM DTT, 1 mM EDTA, pH 6.5, were collected on the 12ID-B SAXS/WAXS beam line at the Advanced Photon Source (APS, Argonne, IL, USA) using a Pilatus 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.08856 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Data were acquired over 30 successive 0.600 second frames from a sample at 2.2 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the radially-averaged solvent-blank was subtracted to produce the scattering profile displayed in this entry.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Beta-crystallin B2
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   23.2 kDa
 
UniProt   P43320
Sequence   FASTA