Human MICAL1: activation by the small GTPase Rab8 and small-angle X-ray scattering studies on the oligomerization state of MICAL1 and its complex with Rab8.

Esposito A, Ventura V, Petoukhov MV, Rai A, Svergun DI, Vanoni MA, Protein Sci (2018) Europe PMC

SASDDR9 – NADPH oxidase (H2O2 producing and [F-actin] oxidizing) MICAL1 (monomer)

[F-actin]-monooxygenase MICAL1 (monomer)
MWexperimental 128 kDa
MWexpected 118 kDa
VPorod 212 nm3
log I(s) 1.70×104 1.70×103 1.70×102 1.70×101
[F-actin]-monooxygenase MICAL1 (monomer) small angle scattering data  s, nm-1
ln I(s)
[F-actin]-monooxygenase MICAL1 (monomer) Guinier plot ln 1.71×104 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
[F-actin]-monooxygenase MICAL1 (monomer) Kratky plot 1.104 0 3 sRg
p(r)
[F-actin]-monooxygenase MICAL1 (monomer) pair distance distribution function Rg: 3.7 nm 0 Dmax: 12.1 nm

Data validation


Fits and models


log I(s)
 s, nm-1
[F-actin]-monooxygenase MICAL1 (monomer) CORAL model

Synchrotron SAXS data, I(s) vs s (where s = 4πsinθ/λ, and 2θ is the scattering angle), were measured from MICAL1 (monomer) using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the EMBL-P12 beam line at the PETRA III storage ring (Hamburg, Germany). Data were collected a using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm. The SEC mobile phase (0.5 ml/min) consisted of 50 mM sodium phosphate buffer, pH 7.5, 5 % glycerol, 100 mM NaCl, 1 mM EDTA, 1 mM DTT, pH 7.5 (23°C). The sample load concentration onto the SEC column was 10 mg/ml (90 µl injection volume). The SAXS data measured from the SEC-elution (sample peak and buffer; 3600 successive 1 s frames) were normalized to the intensity of the transmitted beam and radially averaged. The scattering of an appropriate solvent-blank was subtracted from the sample frames to produce the scaled and averaged data displayed in this entry.

SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN

[F-actin]-monooxygenase MICAL1 (monomer) (Mical1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   117.9 kDa
 
UniProt   Q8TDZ2
Sequence   FASTA