Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages.
Maxwell, Karen L
Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages. [electronic resource] - Journal of bacteriology Dec 2013 - 5461-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1098-5530
10.1128/JB.00805-13 doi
Bacteriophage P2--chemistry
Escherichia coli--virology
Glycoproteins--chemistry
Magnetic Resonance Spectroscopy
Microscopy, Electron
Protein Conformation
Viral Tail Proteins--chemistry
Virion--chemistry
Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages. [electronic resource] - Journal of bacteriology Dec 2013 - 5461-8 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1098-5530
10.1128/JB.00805-13 doi
Bacteriophage P2--chemistry
Escherichia coli--virology
Glycoproteins--chemistry
Magnetic Resonance Spectroscopy
Microscopy, Electron
Protein Conformation
Viral Tail Proteins--chemistry
Virion--chemistry