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

SASDDU9 – NADPH oxidase (H2O2 producing and [F-actin] oxidizing) MICAL1 (monomer) (Truncated MOCH construct)

[F-actin]-monooxygenase MICAL1 (MoCh)

MW^experimental	61	kDa
MW^expected	67	kDa
V^Porod	100	nm³

log I(s) 1.09×10⁴ 1.09×10³ 1.09×10² 1.09×10¹

[F-actin]-monooxygenase MICAL1 (MoCh) small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

[F-actin]-monooxygenase MICAL1 (MoCh) Guinier plot

ln 1.10×10⁴ R_g: 3.4 nm 0 (3.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

[F-actin]-monooxygenase MICAL1 (MoCh) Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 3.5 nm 0 D_max: 12 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.4

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.333
1.080

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

[F-actin]-monooxygenase MICAL1 (MoCh) PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions of the MoCh construct of MICAL1 in 50 mM sodium phosphate buffer, 5 % glycerol, 100 mM NaCl, 1 mM EDTA, 1 mM DTT, pH 7.5 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 (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.47 mg/ml was measured at 15°C. 20 successive 0.050 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.

[F-actin]-monooxygenase MICAL1 (MoCh) (MoCh)
Mol. type		Protein
Organism		Homo sapiens
Olig. state		Monomer
Mon. MW		67.3 kDa

UniProt		Q8TDZ2 (1-614)
Sequence		FASTA

PDB ID		4TXI