Abstract
We investigate the solution structure of human eNOS protein by using synchrotron small-angle X-ray scattering (SAXS). The pair-correlation analysis of the profile shows the radius of gyration (R g ) and maxima dimension (D max ) of 6.87 ± 0.03 nm and 22 nm, respectively. The ratio of D max 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. © 2012 The Physical Society of the Republic of China.