RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins

Methods in Enzymology

Volumn 516, Issue , 2012, Pages 125-152

  Lanz, Nicholas D ^a   Grove, Tyler L ^a   Gogonea, Camelia Baleanu ^a   Lee, Kyung Hoon ^a   Krebs, Carsten ^a   Booker, Squire J ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

AtsB; Cfr; Dehydrogenase; Electron paramagnetic resonance spectroscopy; Iron sulfur cluster; Methylase; M ssbauer spectroscopy; PDB1282; Radical SAM; RlmN; S Adenosylmethionine

Indexed keywords

FLAVODOXIN; FLAVODOXIN REDUCTASE; IRON; OXIDOREDUCTASE; S ADENOSYLMETHIONINE; SULFIDE; SULFUR; UNCLASSIFIED DRUG;

5' UNTRANSLATED REGION; AMINO ACID ANALYSIS; ARTICLE; ATSB GENE; AZOTOBACTER VINELANDII; BINDING SITE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME RECONSTITUTION; ESCHERICHIA COLI; GENE; GENE EXPRESSION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IN VITRO STUDY; IN VIVO STUDY; MOSSBAUER SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RLMN GENE; STOICHIOMETRY; ULTRAVIOLET SPECTROSCOPY;

EID: 84866996636     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394291-3.00030-7     Document Type: Chapter

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