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Title
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Crystallization and preliminary X-ray analysis of the RAD protein from Antirrhinum majus.
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Authors
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C.E.Stevenson,
N.Burton,
M.Costa,
U.Nath,
R.A.Dixon,
E.S.Coen,
D.M.Lawson.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2005,
61,
885-888.
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PubMed id
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Abstract
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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.
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