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Crystallization and preliminary X-ray crystallographic studies on the adenovirus ssDNA binding protein in complex
P N Kanellopoulos1, H van der Zandt, D Tsernoglou
1Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
Abstract:
Crystals of the C-terminal domain of the adenovirus single-stranded DNA binding protein (DBP) in complex with the single-stranded oligonucleotide (dT)16 have been obtained by a batch method from material obtained by chymotryptic digest of full-length DBP. The colorless crystals grow as hexagonal prisms to a maximal size of approximately 0.85 x 0.55 x 0.55 mm. The spacegroup is P3(1)21 with unit cell constants a = 151.5 A and c = 124.0 A. There are either three or four molecules of DBP per asymmetrical unit. To improve the reproducibility of crystallization, recombinant protein has been produced using a baculovirus expression system and shown to crystallize under the same conditions.