Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|65|3|248-252
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.65, Iss.3, 2009-03, pp. : 248-252
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Abstract
Heat‐resistant RNA‐dependent ATPase (Hera) from Thermus thermophilus is a DEAD‐box RNA helicase. Two constructs encompassing the second RecA‐like domain and the C‐terminal domain of Hera were overproduced in Escherichia coli and purified to homogeneity. Single crystals of both Hera constructs were obtained in three crystal forms. A tetragonal crystal form belonged to space group P41212, with unit‐cell parameters a = 65.5, c = 153.0 Å, and contained one molecule per asymmetric unit. Two orthorhombic forms belonged to space group P212121, with unit‐cell parameters a = 62.8, b = 70.9, c = 102.3 Å (form I) and a = 41.6, b = 67.6, c = 183.5 Å (form II). Both orthorhombic forms contained two molecules per asymmetric unit. All crystals diffracted X‐rays to beyond 3 Å resolution, but the tetragonal data sets displayed high Wilson B values and high mean |E2− 1| values, indicating potential disorder and anisotropy. The tetragonal crystal was phased by MAD using a single selenium site.
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