Solution structure and stability of the full-length excisionase from bacteriophage HK022.

Unusual isoaspartyl-glycine linkage at position Asn66-Gly67.

Regulation Of Directionality In Bacteriophage Lambda Site- Specific Recombination: Structure Of The Xis Protein

Solution Structure Of Full-Length Excisionase (Xis) From Bacteriophage Hk022

Bacteriophage Lambda Excisionase (Xis)-Dna Complex

Structure Of The Cooperative Excisionase (Xis)-Dna Complex Reveals A Micronucleoprotein Filament

Crystal Structure Of The Lambda Xis-Dna Complex

excisionase [Escherichia coli O157:H7 str. Sakai]

putative excisionase [Escherichia coli O26:H11 str. 11368]

excisionase [Escherichia coli O26:H11 str. 11368]

predicted excisionase [Escherichia coli O111:H- str. 11128]

unnamed protein product [Enterobacteria phage HK022]

excisionase-like protein [Enterobacteria phage H19J]

predicted excisionase [Escherichia coli O127:H6 str. E2348/69]

xis (excision;72) [Enterobacteria phage lambda]

excisionase [Enterobacteria phage HK022]

Excisionase [Enterobacteria phage lambda]

MULTISPECIES: excisionase [Enterobacteriaceae]

RecName: Full=Excisionase [Enterobacteria phage lambda]

RecName: Full=Excisionase [Enterobacteria phage HK022]

Solution Structure and Stability of the Full-Length Excisionase (Xis) from Bacteriophage HK022