Crystallization and preliminary X-ray crystallographic studies on the adenovirus ssDNA binding protein in complex with ssDNA.
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.
Kanellopoulos
P N
PN
Structural Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
van der Zandt
H
H
Tsernoglou
D
D
van der Vliet
P C
PC
Tucker
P A
PA
D001483:Base Sequence; D002845:Chromatography; D002918:Chymotrypsin / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004277:DNA, Single-Stranded / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D011071:Poly T / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
C095599:DBP protein, Adenovirus; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D014764:Viral Proteins; D011071:Poly T; D002918:Chymotrypsin