Globin sensor domain of AfGcHK (FeIII form) in complex with cyanide

Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction.

AfGcHK,Heme-based oxygen-sensor histidine kinase

Crystal shape - red wedge block 300x80x80 um

20.7% (w/v) PEG3350, 200 mM MgCl2, 0.01 M KCN, 7.5% (v/v) glycerol, 0.1 M MMT buffer system (DL-Malic acid, MES monohydrate, Tris, NaOH, HCl), pH 6.7

Ministry of Education, Youth and Sports of the Czech Republic

Grant Agency of the Czech Technical University

Rg from SAXS: 22A, Rg from structure coordinates for dimer: 20A

- column - Superdex 200
- buffer 20mM Tris, 150mM NaCl, pH 8,0
- molecular mass in solution (by gel filtration) - 40000 Da (calibrated by ovalbumin - 43 kDa, bovie serum albumin - 66 kDa, aldolase - 158 kDa)
- molecular mass according to aminoacid sequence - 18341 Da

Analytical ultracentrifugation:
buffer 20mM Tris, 150mM NaCl, pH 8,0
sw=3,090 and sw(20,w)=3.207
molecular mass in solution (by AUC) - 38999 Da
molecular mass according to amino acid sequence - 18341 Da

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

Globin-coupled histidine kinase (E.C.2.7.13.3)

Heme, Sensor protein, Oxygen sensor, Globin sensor domain, globin domain, cyanide, transferase