crystal structure of a complex of soluble angiotensin-converting enzyme 2 (ACE2), residues 19 to 615 and SARS-CoV spike protein receptor binding domain (RBD), residues 306 to 575. Crystals in space group P21, a = 82.3 A, b = 119.4 A, c = 113.2 A, beta = 91.2°, with two complexes per asymmetric unit, are grown at room temperature from a mother liquor containing 24% polyethylene glycol 6000, 150 mM NaCl, 100 mM Tris at pH 8.2, and 10% ethylene glycol. The crystal structure at 2.9 A resolution of the RBD of the SARS-CoV spike protein bound with the peptidase domain of human ACE2 shows that the RBD presents a gently concave surface, which cradles the N-terminal lobe of the peptidase
hanging drop vapor diffusion at 16-18°C, crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains are solved to 2.2 A and 3.0 A resolution; hanging drop vapor diffusion at 16-18°C, crystal structures of the native and inhibitor(MLN-4760)-bound forms of the ACE2 extracellular domains are solved to 2.2 and 3.0 A resolution, respectively
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