Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima.

Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G, Structure 25(12):1887-1897.e4 (2017) Europe PMC

SASDCC7 – Thermotoga martitima phosphodiesterase TM1595 D80N D154N (inactive mutant)

T.maritima PDE
MWexperimental 72 kDa
MWexpected 76 kDa
VPorod 115 nm3
log I(s) 9.29×103 9.29×102 9.29×101 9.29×100
T.maritima PDE small angle scattering data  s, nm-1
ln I(s)
T.maritima PDE Guinier plot ln 9.29×103 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
T.maritima PDE Kratky plot 1.104 0 √3 sRg
p(r)
T.maritima PDE pair distance distribution function Rg: 2.8 nm 0 Dmax: 7.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Thermotoga martitima phosphodiesterase TM1595 D80N D154N (inactive mutant) in 25mM Tris 500mM NaCl 3% (v/v) glycerol 2mM MgCl2, pH 8, were collected on the EMBL-P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). Samples were collected using SEC-SAXS at 20°C. The scattering was obtained by averaging the main peak's scattering data of a SECSAXS run with TmPDE D80ND154N on a 10/300 S200 superdex column. The data was corrected for buffer scattering by subtraction of an averaged buffer region using the CHROMIXS software (ATSAS 2.8.1).

Number of frames = UNKNOWN. Concentration = UNKNOWN

T.maritima PDE (TmPDE D80N D154N)
Mol. type   Protein
Organism   Thermotoga maritima
Olig. state   Dimer
Mon. MW   37.8 kDa
 
UniProt   Q9X1T1
Sequence   FASTA