Crystal structures of substrate-bound chitinase from the psychrophilic bacterium Moritella marina and its structure in solution.

Malecki PH, Vorgias CE, Petoukhov MV, Svergun DI, Rypniewski W, Acta Crystallogr D Biol Crystallogr 70(Pt 3):676-84 (2014) Europe PMC

SASDAP4 – Chitinase 60 from Moritella marina

Chitinase 60
MWexperimental 50 kDa
MWexpected 61 kDa
VPorod 75 nm3
log I(s) 2.85×103 2.85×102 2.85×101 2.85×100
Chitinase 60 small angle scattering data  s, nm-1
ln I(s)
Chitinase 60 Guinier plot ln 2.85×103 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Chitinase 60 Kratky plot 1.104 0 √3 sRg
p(r)
Chitinase 60 pair distance distribution function Rg: 3.4 nm 0 Dmax: 11.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Chitinase 60 from Moritella marina Rg histogram Rg, nm
Chitinase 60 EOM/RANCH model
Chitinase 60 EOM/RANCH model
Chitinase 60 EOM/RANCH model
Synchrotron SAXS data from solutions of Chitinase 60 from Moritella marina in 20 mM Tris 200 mM NaCl, pH 8 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 8.8 mg/ml were measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

The fit is obtained by the average of three EOM models

Chitinase 60
Mol. type   Protein
Organism   Moritella marina
Olig. state   Monomer
Mon. MW   60.8 kDa
 
UniProt   B1VBB0
Sequence   FASTA