Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.

Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T, Biochemistry 55(6):914-26 (2016) Europe PMC

SASDBH3 – Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 (fragment 30-380)

Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2
MWexperimental 88 kDa
MWexpected 80 kDa
log I(s) 6.74×101 6.74×100 6.74×10-1 6.74×10-2
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 small angle scattering data  s, nm-1
ln I(s)
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 Guinier plot ln 6.74×101 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 Kratky plot 1.104 0 √3 sRg
p(r)
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 pair distance distribution function Rg: 4.5 nm 0 Dmax: 21.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 DAMMIN model
X-ray synchrotron radiation scattering data from solutions of Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 in 20 mM Tris 150 mM NaCl, 3% glycerol were collected on the ID14-3 beam line at the ESRF storage ring (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 1.30-3.40 mg/ml were measured. 10 successive 1 second frames were collected at a sample temperature of 10 degrees centigrade. SAXS data from the samples and corresponding matched solvent blank were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The SAXS data for this entry were derived from the concentration series extrapolated to infinite dilution.

Cell temperature = UNKNOWN

Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 (LRRTM2 30-380)
Mol. type   Protein
Organism   Mus musculus
Olig. state   Dimer
Mon. MW   40.1 kDa
 
UniProt   Q8BGA3 (30-380)
Sequence   FASTA