Journal: Nucleic Acids Research

Article Title: RNase W, a conserved ribonuclease family with a novel active site

doi: 10.1093/nar/gkae907

Figure Lengend Snippet: X-ray diffraction and refinement statistics

Article Snippet: The open reading frames of RNase W (FAU-1) from P. furiosus (full-length protein, constructs and mutants; PF0022) and S. acidocadarius (Saci_1213) were synthesized commercially by GenScript Corp. (Piscatawy, NJ) and inserted in pET24(a+) (Novagen), pET24- Pf RNase W and pET24- Sa RNase W, respectively.

Techniques: X-ray Diffraction

Journal: Nucleic Acids Research

Article Title: RNase W, a conserved ribonuclease family with a novel active site

doi: 10.1093/nar/gkae907

Figure Lengend Snippet: Structures of RNase W from P. furiosus and S. acidocaldarius . ( A and B ) Structures of RNase W proteins colored by domains: N-terminal domain in orange, S1 domain in dark green, 5′-sensor domain in light green, α helical bundle domain in red and DUF402 domain in blue. ( A ) Structure of RNase W from P. furiosus ( Pf RNase W). A dinucleotide UU with 5′ and 3′-phosphate extremities is bound to the 5′-sensor domain. In addition, a dinucleotide UA with 5′-hydroxyl and 3′-phosphate extremities is bound to the DUF402 domain. ( B ) Structure of RNase W from S. acidocaldarius ( Sa RNase W). ( C ) Pf RNase W surface representation with residues conservation score in archaeal RNase W proteins mapped on the surface. The encircled central domain includes the N-terminal domain and one helix of the α helical bundle domain annotated in panel A. ( D ) Electrostatic surface potential mapped on the surface of Pf RNase W protein.

Article Snippet: The open reading frames of RNase W (FAU-1) from P. furiosus (full-length protein, constructs and mutants; PF0022) and S. acidocadarius (Saci_1213) were synthesized commercially by GenScript Corp. (Piscatawy, NJ) and inserted in pET24(a+) (Novagen), pET24- Pf RNase W and pET24- Sa RNase W, respectively.

Techniques: