Recombinant AcnB, NrdR and RibD of Acinetobacter baumannii and their potential interaction with DNA adenine methyltransferase AamA.

Weber K, Doellinger J, Jeffries CM, Wilharm G, Protein Expr Purif :106134 (2022) Europe PMC

SASDNF5 – Acinetobacter baumannii transcriptional repressor NrdR (likely filamentous assembly)

Transcriptional repressor NrdR
MWexperimental 1000 kDa
MWexpected 19 kDa
log I(s) 3.73×10-1 3.73×10-2 3.73×10-3 3.73×10-4
Transcriptional repressor NrdR small angle scattering data  s, nm-1
ln I(s)
Transcriptional repressor NrdR Guinier plot ln 3.73×10-1 Rg: 19.9 nm 0 (19.9 nm)-2 s2
Transcriptional repressor NrdR Kratky plot 1.104 0 3 sRg
Transcriptional repressor NrdR pair distance distribution function Rg: 23.8 nm 0 Dmax: 92.6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of the filamentous assembly of NrdR in 100 mM NaCl, 20 mM Tris, 1 mM DTT, 3% v/v glycerol, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.40 mg/ml was measured at 20°C. 62 successive 0.100 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.

Appears as a large filamentous assembly, therefore the molecular weight is indeterminate, ranging above 500 kDa. The recombinant protein contains a N-terminal hexa-histidine amino acid protein affinity chromatography tag (HHHHHHLE). The p(r) profile estimation of Dmax should be interpreted only as an approximation.

Transcriptional repressor NrdR (NdnR)
Mol. type   Protein
Organism   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Olig. state   Unknown
Mon. MW   18.9 kDa
UniProt   A3M1A1 (1-152)
Sequence   FASTA