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

scientific article published on 01 July 1994

2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1038/NSB0794-461
P953full work available at URLhttp://www.nature.com/articles/nsb0794-461.pdf
http://www.nature.com/articles/nsb0794-461
P698PubMed publication ID7664065

P50authorMichael J. BenedikQ42207564
Mitchell D MillerQ87708776
P2093author name stringJ. Tanner
K. L. Krause
M. Alpaugh
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Cloning and expression in Escherichia coli of the gene for extracellular phospholipase A1 from Serratia liquefaciensQ36428503
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X-ray structure of the DNase I-d(GGTATACC)2 complex at 2.3 A resolutionQ38326595
Serratia bacteremia: review of 118 casesQ38509316
Lipolytic activity copurified with the outer membrane of Serratia marcescensQ39973024
Relation between structure and function of alpha/beta-proteinsQ40304064
The extracellular nuclease gene of Serratia marcescens and its secretion from Escherichia coliQ48352221
Acetylcholinesterase: electrostatic steering increases the rate of ligand binding.Q52402262
Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNAQ59092559
Electrostatics and diffusion of molecules in solution: simulations with the University of Houston Brownian dynamics programQ61773837
Crystallization and preliminary crystallographic analysis of a novel nuclease from Serratia marcescensQ68261725
Point charge distributions and electrostatic steering in enzyme/substrate encounter: Brownian dynamics of modified copper/zinc superoxide dismutasesQ68616814
Stereochemically restrained refinement of macromolecular structuresQ69806243
Evaluation of single-crystal X-ray diffraction data from a position-sensitive detectorQ107329121
P433issue7
P407language of work or nameEnglishQ1860
P921main subjectmolecular modelQ2196961
P304page(s)461-468
P577publication date1994-07-01
P1433published inNature structural biologyQ26842658
P1476title2.1 A structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
P478volume1

Reverse relations

cites work (P2860)
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