2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA


The crystal structure of Serratia endonuclease has been solved to 2.1 Å by multiple isomorphous replacement. This magnesium-dependent enzyme is equally active against single- and double-stranded DNA, as well as RNA, without any apparent base preference. The Serratia endonuclease fold is distinct from that of other nucleases that have been solved by X-ray… (More)
DOI: 10.1038/nsb0794-461