Four crystal forms of a Bence-Jones protein.
- Author(s): Makino, Debora L;
- Henschen-Edman, Agnes H;
- McPherson, Alexander
- et al.
Published Web Locationhttps://doi.org/10.1107/s1744309104028532
Four crystal forms have been grown and characterized by X-ray diffraction of a Bence-Jones protein collected from the urine of a multiple myeloma patient more than 40 years ago. Closely related tetragonal and orthorhombic forms belonging to space groups P4(3)2(1)2 and P2(1)2(1)2(1), with unit-cell parameters a = b = 68.7, c = 182.1 and a = 67.7, b = 69.4, c = 87.3 A, diffract to 1.5 and 1.9 A, respectively. Two closely related trigonal forms, both belonging to space group P3(1)21 with unit-cell parameters a = b = 154.3 A but differing by a doubling of the c axis, one 46.9 A and the other 94.0 A, diffract to 2.9 and 2.6 A resolution, respectively. The trigonal crystal of short c-axis length shows a positive indication of twinning. The trigonal crystal of longer c axis, which appeared only after eight months of incubation at room temperature, is likely to be composed of proteolytically degraded molecules and unlike the other crystal forms contains two entire Bence-Jones dimers in the asymmetric unit. This latter crystal form may shed some light on the formation of fibrils common to certain storage diseases.