Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase.

Van Laer B, Kapp U, Soler-Lopez M, Moczulska K, Pääbo S, Leonard G, Mueller-Dieckmann C, Sci Rep 8(1):18008 (2018) Europe PMC

SASDEL5 – AICAR-bound human adenylosuccinate lyase (ADSL)

Adenylosuccinate Lyase
MWexperimental 165 kDa
MWexpected 221 kDa
VPorod 291 nm3
log I(s) 1.53×102 1.53×101 1.53×100 1.53×10-1
Adenylosuccinate Lyase small angle scattering data  s, nm-1
ln I(s)
Adenylosuccinate Lyase Guinier plot ln 1.53×102 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Adenylosuccinate Lyase Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of AICAR-bound human adenylosuccinate lyase (ADSL) in 10 mM HEPES, 100 mM NaCl, 1 mM DTT, 1 mM 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR), pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Dectris Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. 10 successive 1 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.

Adenylosuccinate Lyase (ADSL)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   55.2 kDa
 
UniProt   P30566 (1-484)
Sequence   FASTA