Increased association between Epstein-Barr virus EBNA2 from type 2 strains and the transcriptional repressor BS69 restricts B cell growth

Ponnusamy R, Khatri R, Correia P, Mancini E, Farrell P, West M, (2018) DOI

SASDEH6 – BS69 (CC-MYND: Zinc finger MYND domain-containing protein 11, amino acids 480-602)

Zinc finger MYND domain-containing protein 11
MWexperimental 67 kDa
MWexpected 60 kDa
VPorod 83 nm3
log I(s) 9.62×10-2 9.62×10-3 9.62×10-4 9.62×10-5
Zinc finger MYND domain-containing protein 11 small angle scattering data  s, nm-1
ln I(s)
Zinc finger MYND domain-containing protein 11 Guinier plot ln 9.63×10-2 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
Zinc finger MYND domain-containing protein 11 Kratky plot 1.104 0 3 sRg
p(r)
Zinc finger MYND domain-containing protein 11 pair distance distribution function Rg: 5.3 nm 0 Dmax: 16.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Zinc finger MYND domain-containing protein 11 DAMMIN model
Zinc finger MYND domain-containing protein 11 DAMMIF model

Synchrotron SAXS data from solutions of BS69 (CC-MYND: Zinc finger MYND domain-containing protein 11, amino acids 480-602) in 20mM Tris-HCl, 100mM NaCl, 2% Sucrose and 1mM TCEP, pH 7.5 were collected on the B21 beam line at the Diamond Light Source storage ring (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The sample was measured using size exclusion chromatography SAXS (SEC-SAXS) at 25°C. 30 successive 3 second frames were collected through the SEC sample elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of an appropriate solvent-blank was subtracted.

SEC-SAXS was performed using the following parameters: Column type: S200 3.2/300 increase; Flow rate: 0.075 ml/min; Injection volume: 45 µl; Sample injection concentration: 15.0 mg/ml.

Zinc finger MYND domain-containing protein 11 (BS69 CC-MYND)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   15.1 kDa
 
UniProt   Q15326-1 (480-602)
Sequence   FASTA