@article {333,
	title = {Crystallization and preliminary X-ray diffraction of the DEAD-box protein Mss116p complexed with an RNA oligonucleotide and AMP-PNP.},
	journal = {Acta Crystallogr Sect F Struct Biol Cryst Commun},
	volume = {65},
	number = {Pt 8},
	year = {2009},
	month = {2009 Aug 1},
	pages = {832-5},
	abstract = {The Saccharomyces cerevisiae DEAD-box protein Mss116p is a general RNA chaperone which functions in mitochondrial group I and group II intron splicing, translation and RNA-end processing. For crystallization trials, full-length Mss116p and a C-terminally truncated protein (Mss116p/Delta598-664) were overproduced in Escherichia coli and purified to homogeneity. Mss116p exhibited low solubility in standard solutions (< or =1 mg ml(-1)), but its solubility could be increased by adding 50 mM L-arginine plus 50 mM L-glutamate and 50\% glycerol to achieve concentrations of approximately 10 mg ml(-1). Initial crystals were obtained by the microbatch method in the presence of a U(10) RNA oligonucleotide and the ATP analog AMP-PNP and were then improved by using seeding and sitting-drop vapor diffusion. A cryocooled crystal of Mss116p/Delta598-664 in complex with AMP-PNP and U(10) belonged to space group P2(1)2(1)2, with unit-cell parameters a = 88.54, b = 126.52, c = 55.52 A, and diffracted X-rays to beyond 1.9 A resolution using synchrotron radiation from sector 21 at the Advanced Photon Source.},
	keywords = {Adenylyl Imidodiphosphate, Cloning, Molecular, Crystallization, Crystallography, X-Ray, DEAD-box RNA Helicases, Molecular Conformation, Recombinant Proteins, RNA, Saccharomyces cerevisiae Proteins},
	issn = {1744-3091},
	doi = {10.1107/S1744309109027225},
	author = {Del Campo, Mark and Lambowitz, Alan M}
}
