Four crystal forms of a Bence-Jones protein

Autor: Agnes H. Henschen-Edman, Alexander McPherson, Debora L. Makino
Rok vydání: 2004
Předmět:
Zdroj: Makino, DL; Henschen-Edman, AH; & McPherson, A. (2005). Four crystal forms of a Bence-Jones protein. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 61(1), 79-82. doi: 10.1107/S1744309104028532. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/6h80f902
ISSN: 1744-3091
Popis: 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 P43212 and P212121, with unit-cell parameters a = b = 68.7, c = 182.1 and a = 67.7, b = 69.4, c = 87.3 Å, diffract to 1.5 and 1.9 Å, respectively. Two closely related trigonal forms, both belonging to space group P3121 with unit-cell parameters a = b = 154.3 Å but differing by a doubling of the c axis, one 46.9 Å and the other 94.0 Å, diffract to 2.9 and 2.6 Å 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. © 2005 International Union of Crystallography All rights reserved.
Databáze: OpenAIRE