title: Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein BstDEAD from Bacillus stearothermophilus.
abstract: DEAD proteins are members of a large and diverse family of RNA helicases that use energy from ATP hydrolysis to unwind short regions of duplex RNA. BstDEAD from Bacillus stearothermophilus is a 436-amino-acid protein and a representative member of the DEAD protein family. In addition to the mechanistic core common to DEAD proteins, BstDEAD has a unique approximately 60-amino-acid C-terminal extension that may denote a specific biological role. BstDEAD has been crystallized in space group P4(1/3)2(1)2, with unit-cell parameters a = b = 100.3, c = 110.6 A and one molecule per asymmetric unit. It is the first DEAD protein to be crystallized containing a unique extension outside of the core.
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D053487:DEAD-box RNA Helicases; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D020365:RNA Helicases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
chemical_list: D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; C088840:deaD protein, E coli; D053487:DEAD-box RNA Helicases; D020365:RNA Helicases