Abstract: We investigate the solution structure of human eNOS protein by using synchrotron smallangle
X-ray scattering (SAXS). The pair-correlation analysis of the profile shows the radius
of gyration (Rg) and maxima dimension (Dmax) of 6.87 ± 0.03 nm and 22 nm, respectively.
The ratio of Dmax and Rg revealed that the protein was an extended conformation. The
ab initio shape determination and rigid-body calculations were performed to reconstruct
the real-space structure of eNOS in solution. The result shows that human eNOS form
homodimer form in solution with the closed contact of two oxygenase domains.