Crystallization of a human Bence-Jones protein in microgravity using vapordiffusion in capillaries

A simple evaporative method in sealed capillaries was used to produce X-ray diffraction quality crystals of a monoclonal human Bence-Jones protein (Se a) in microgravity and at unit gravity. The lambda isotypic Bence-Jones pro tein was purified from the urine of a multiple myeloma patient using ammoni um sulfate precipitation, dialysis and cation exchange, followed by gel fil tration. Crystals were produced in glass capillaries where water evaporated from the protein solution was absorbed by one or two suitable absorbents. A crystal grown during the 9-day Space Shuttle STS-95 flight measured 8 x 1 .6 x 1 mm. It was subjected to X-ray diffraction and was found to be orthor hombic (P2(1)2(1)2(1)). With unit-cell dimensions of 48.9, 85.2 and 114.0 A ngstrom. X-ray data were collected at room temperature and were 98.3% compl ete to 2.3 Angstrom resolution. Crystals of the same Bence-Jones protein me asuring 1.2-2 mm in length were grown in ground-based controls using a high evaporation rate for the first 12 h, followed by a slower evaporation rate for the remainder of the 19-day growth period, (C) 2001 Elsevier Science B .V, All rights reserved.