EC Number   |
|---|
    6.6.1.1 | multiple wavelength anomalous dispersion method |
| 6.6.1.1 | subunit BchH, at 25 A resolution. The apo structure contains three major lobe-shaped domains connected at a single point with additional densities at the tip of two lobes termed the thumb and finger. The substrate-bound BchH complex BchH Proto shows a distinct conformational change in the thumb and finger subdomains. Prolonged proteolysis of native apo-BchH produces a stable C-terminal fragment of 45 kDa, and protoporphyrin protects the full-length polypeptide from degradation |
| 6.6.1.1 | using electron microscopy and small-angle x-ray scattering the structure of ChlH subunit is investigated. ChlH is a large, 148-kDa protein of 1326 residues, forming a cage-like assembly comprising the majority of the structure, attached to a globular N-terminal domain of 16 kDa by a narrow linker region. This N-terminal domain is adjacent to a 5 nm-diameter opening in the structure that allows access to a cavity |
| 6.6.1.1 | vapor diffusion method, using 0.85 M sodium citrate, pH 7.0 and 2 mM dithiothreitol |
