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Abstract A human l-type Bence-Jones protein (Mcg) was crystallized from water in a form suitable for x-ray diffraction studies. The crystals were composed of one molecular species of the protein, M-S-S-M, representing two identical polypeptide chains (M) linked by a disulfide bond. The protein crystallized in the orthorhombic space group P21212. Four M-S-S-M molecules were present in the unit cell, the dimensions of which were: a = 72.6 ± 0.2; b = 81.9 ± 0.2; and c = 71.0 ± 0.2 A. The crystallographic asymmetric unit was the M-S-S-M dimer.
Schiffer et al. (Sun,) studied this question.