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Updated: Aug 31, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Purification, crystallization and preliminary X-ray analysis of the novel DEAD protein BstDEAD from Bacillus
Andrew B Carmel1, Brian W Matthews
1Institute of Molecular Biology, Howard Hughes Medical Institute and Departments of Chemistry and Physics, 1229 University of Oregon, Eugene, OR 97403-1229, USA.
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.
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