Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 61, Part 10 (October 2005)

crystallization communications

Acta Cryst. (2005). F61, 885-888 [ doi:10.1107/S1744309105027168 ]

Crystallization and preliminary X-ray analysis of the RAD protein from Antirrhinum majus

C. E. M. Stevenson, N. Burton, M. Costa, U. Nath, R. A. Dixon, E. S. Coen and D. M. Lawson

Abstract: Crystals of the RADIALIS protein from Antirrhinum majus were grown by vapour diffusion after limited proteolysis. Mass spectrometry indicated that an 8 kDa fragment had been crystallized corresponding to the predicted MYB DNA-binding domain. X-ray data collected at room temperature were consistent with tetragonal symmetry, whereas data collected at 100 K using crystals cryoprotected by supplementing the mother liquor with ethylene glycol conformed to orthorhombic symmetry. It was subsequently shown that crystals soaked in cryoprotectants that were `osmolality-matched' to the mother liquor retained tetragonal symmetry. Using these crystals, X-ray data were collected in-house to a maximum resolution of 2 Å.

Keywords: RADIALIS; limited proteolysis; osmolality.