X-ray Crystal Structure of Chemically Synthesized Crambin-{alpha}carboxamide
Role of a salt bridge in the model protein crambin explored by chemical protein synthesis: X-ray structure of a unique protein analogue, [V15A]crambin-alpha-carboxamide.
X-ray crystallography-quality crystals for crambin-carboxamide were formed by mixing 2 ul of protein (10 mg/ml in pH 7.5 100mM HEPES buffer containing 150 mM NaCl) and 2 ul of a 0.8 M succinic acid (used for X-ray diffraction), or by mixing 2 ul of the protein solution with 2 ul of 0.1 M HEPES buffer containing 15% v/v tacsimate and 2% w/v polyethylene glycol 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
The protein was chemically synthesized. The sequence of the protein can be naturally found in Crambe abyssinica (Abyssinian crambe).
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS