id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-294679-7pklrmz5	Wei, Lei	Purification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domain	2008-08-09		.txt	text/plain	1069	73	61	title: Purification, crystallization and preliminary crystallographic analysis of avian infectious bronchitis virus nsp3 ADRP domain Avian infectious bronchitis virus (IBV) encodes 15 nonstructural proteins (nsps) which play crucial roles in RNA transcription and genome replication. One of them, nsp3, contains an ADRP (adenosine diphosphate-ribose-1′-phosphatase) domain which was revealed in recent studies to have ADP-ribose-1′-monophos­phatase (Appr-1′-pase) activity. The gene segment encoding the IBV nsp3 ADRP domain has been cloned and expressed in Escherichia coli. Considering that the genomes encoding the nonstructural proteins (nsps) are conserved among SARS-Cov, IBV, human-Cov 229E etc., the study of IBV will facilitate the thorough understanding of coronaviruses. Initial crystals were obtained from Index Screen condition No. 84 containing 0.2 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 25%(w/v) polyethylene glycol 3350. A typical diffraction pattern of an IBV nsp3 ADRP domain crystal collected on a Rigaku R-AXIS IV ++ image-plate detector. Avian infectious bronchitis virus nsp3	./cache/cord-294679-7pklrmz5.txt	./txt/cord-294679-7pklrmz5.txt