title: Crystallization and preliminary X-ray analysis of the RAD protein from Antirrhinum majus.
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 A.
authors.affiliation: Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, England.
authors.forename: Clare E M
authors.initials: CE
authors.lastname: Stevenson
authors.forename: Nicolas
authors.initials: N
authors.lastname: Burton
authors.forename: Manuela
authors.initials: M
authors.lastname: Costa
authors.forename: Utpal
authors.initials: U
authors.lastname: Nath
authors.forename: Ray A
authors.initials: RA
authors.lastname: Dixon
authors.forename: Enrico S
authors.initials: ES
authors.lastname: Coen
authors.forename: David M
authors.initials: DM
authors.lastname: Lawson
mesh_terms: D032161:Antirrhinum / Q000378:metabolism*; D015925:Cryopreservation; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry; D004058:Diffusion; D004591:Electrophoresis, Polyacrylamide Gel; D019855:Ethylene Glycol / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013696:Temperature; D014157:Transcription Factors / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D014157:Transcription Factors; D004247:DNA; D019855:Ethylene Glycol