Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.

Korasick DA, Končitíková R, Kopečná M, Hájková E, Vigouroux A, Moréra S, Becker DF, Šebela M, Tanner JJ, Kopečný D
J Mol Biol (2018 Dec 20)
PMID: 30580036
doi: 10.1016/j.jmb.2018.12.010
Submitted to SASBDB: 2018 Oct 9
Published in SASBDB:

SASDE96 – Aldehyde dehydrogenase 12 from Zea mays Extrapolated to Infinite Dilution

Aldehyde dehydrogenase 12 experimental SAS data
ALLOSMOD model
Sample: Aldehyde dehydrogenase 12 tetramer, 242 kDa Zea mays protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM TCEP, and 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Dec 6
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 351 nm3