Structural Analysis of Pathogenic Mutations Targeting Glu427 of ALDH7A1, the Hot Spot Residue of Pyridoxine-Dependent Epilepsy.

Laciak AR, Korasick DA, Gates KS, Tanner JJ, J Inherit Metab Dis (2019) Europe PMC

SASDGU4 – Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399G at 6.5 mg/mL

Alpha-aminoadipic semialdehyde dehydrogenase E399G
MWexperimental 205 kDa
MWexpected 55 kDa
VPorod 270 nm3
log I(s) 1.03×102 1.03×101 1.03×100 1.03×10-1
Alpha-aminoadipic semialdehyde dehydrogenase E399G small angle scattering data  s, nm-1
ln I(s)
Alpha-aminoadipic semialdehyde dehydrogenase E399G Guinier plot ln 1.04×102 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Alpha-aminoadipic semialdehyde dehydrogenase E399G Kratky plot 1.104 0 √3 sRg
Dmax: 10 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Alpha-aminoadipic semialdehyde dehydrogenase E399G PDB (PROTEIN DATA BANK) model
Alpha-aminoadipic semialdehyde dehydrogenase E399G PDB (PROTEIN DATA BANK) model
Synchrotron SAXS data from solutions of Human alpha-aminoadipic semialdehyde dehydrogenase (ALDH)7A1 E399G at 6.5 mg/mL in 50 mM HEPES, 100 mM NaCl, 1 mM DTT, 10 mM NAD, 2% (v/v) glycerol, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.50 mg/ml was 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.

X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Alpha-aminoadipic semialdehyde dehydrogenase E399G (ALDH7A1 E399G)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   55.5 kDa
 
UniProt   P49419
Sequence   FASTA
 
PDB ID   4ZUK
 
PDB ID   4ZUK