id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-261110-cnj0e0s9	Debarnot, Claire	Crystallization and diffraction analysis of the SARS coronavirus nsp10–nsp16 complex	2011-02-25		.txt	text/plain	2656	169	64	This positive RNA virus encodes a large replicase polyprotein made up of 16 gene products (nsp1–16), amongst which two methyltransferases, nsp14 and nsp16, are involved in viral mRNA cap formation. We present X-ray diffraction data from these SARS-CoV nsp10-nsp16 crystals. The purified SARS-CoV nsp10-nsp16 complex was analyzed by 12% SDS-PAGE and stained using Coomassie Blue. Lane MK, molecular-weight markers; lane 1, 2 mg nsp10-nsp16 protein complex eluted from the Strep-Tactin column. The nsp10-nsp16 complex eluted from the Strep-Tactin column was analyzed on a 16/60 S200 gel-filtration column and the elution of protein and nucleic acid was followed by measuring the absorption at 280 nm (blue) and 260 nm (orange), respectively. The purified SARS-CoV nsp10-nsp16 complex was loaded onto a 4-12% NuPAGE gel and stained using Coomassie Blue. We have crystallized a complex of the SARS-CoV nsp10 and nsp16 proteins.	./cache/cord-261110-cnj0e0s9.txt	./txt/cord-261110-cnj0e0s9.txt