Crystal and solution structures of the helicase-binding domain of escherichia coli primase*

HIGHLIGHTS

• who: Aaron J. Oakley from the (UNIVERSITY) have published the research work: Crystal and Solution Structures of the Helicase-binding Domain of Escherichia coli Primase*, in the Journal: (JOURNAL) of December/22,/2004
• what: The authors demonstrate directly by surface plasmon resonance that the C-terminal domain of primase is responsible for interaction with DnaB6.
• how: The authors used a 3⬘-biotinylated oligonucleotide (3⬘Bio-(dT)35) long enough that it should bind well within the central channel of the helicase but not projecting so far that it could simultaneously interact with DnaB6 . . .
  

   

  

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