FHL2 production enabled new insight into its flexibility and unexpected binding stoichiometry with β-catenin.

Logonder T Prešern U, Gaber A, J Struct Biol X 14:100159 (2026) Europe PMC

SASDZ36 – Full-length tag-free Four and a half LIM domains protein 2 (FHL2), 7.5 mg/ml

Four and a half LIM domains protein 2
MWexperimental 28 kDa
MWexpected 32 kDa
VPorod 43 nm3
log I(s) 2.96×103 2.96×102 2.96×101 2.96×100
Four and a half LIM domains protein 2 small angle scattering data  s, nm-1
ln I(s)
Four and a half LIM domains protein 2 Guinier plot ln 2.97×103 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Four and a half LIM domains protein 2 Kratky plot 1.104 0 3 sRg
p(r)
Four and a half LIM domains protein 2 pair distance distribution function Rg: 3.9 nm 0 Dmax: 13.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Full-length tag-free Four and a half LIM domains protein 2 (FHL2), 7.5 mg/ml in 20 mM HEPES, 150 mM NaCl, 5 % (v/v) glycerol, 10 mM β-mercaptoethanol, pH 7.4 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.137759 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 7.5 mg/ml was injected at a 0.70 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 3000 successive 0.995 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.

Four and a half LIM domains protein 2 (FHL2)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   32.1 kDa
 
UniProt   Q14192 (1-279)
Sequence   FASTA