Solution structures of long-acting insulin analogues and their complexes with albumin.

Ryberg LA, Sønderby P, Barrientos F, Bukrinski JT, Peters GHJ, Harris P, Acta Crystallogr D Struct Biol 75(Pt 3):272-282 (2019) Europe PMC

SASDEV5 – Insulin detemir tri-hexamer

Insulin detemir
MWI(0) 100 kDa
MWexpected 106 kDa
VPorod 137 nm3
log I(s) 7.20×10-2 7.20×10-3 7.20×10-4 7.20×10-5
Insulin detemir small angle scattering data  s, nm-1
ln I(s)
Insulin detemir Guinier plot ln 7.20×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Insulin detemir Kratky plot 1.104 0 √3 sRg
p(r)
Insulin detemir pair distance distribution function Rg: 3.4 nm 0 Dmax: 11.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Insulin detemir SASREF CV model
log I(s)
 s, nm-1
Insulin detemir DAMMIF model
Synchrotron SAXS data from solutions of insulin detemir tri-hexamer in 5.0 mM Na2HPO4, 13.1 mM m-cresol, 15.1 mM phenol, 173.7 mM glycerol, 20.0 mM NaCl, pH 7.4 were collected on the I911-4 beam line at the MAX IV storage ring (Lund, Sweden) using a Dectris Pilatus 1M detector at a sample-detector distance of 2.0 m and at a wavelength of λ = 0.091 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.50 mg/ml was measured at 20°C. Four successive 30 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.

Storage temperature = UNKNOWN

Insulin detemir
Mol. type   Protein
Olig. state   18-mer
Mon. MW   5.9 kDa
 
UniProt   P01308 (25-110)
Sequence   FASTA
 
PDB ID   1TRZ