title: Fast preparative separation of 'native' core E coli 30S ribosomal proteins.
abstract: We have developed an ion-exchange high performance liquid chromatographic method for preparative separation of 'core' proteins from E coli 30S ribosomal subunits, extracted with salt under non-denaturing conditions. This method yields individual proteins in pure and native form at high concentrations, (5 to 25 mg/ml) suitable for direct use in 1D-, 2D- or 3D-NMR studies.
authors.affiliation: Laboratoire de Biophysique, UFR des Sciences Pharmaceutiques et Biologiques, Dijon, France.
authors.forename: C
authors.initials: C
authors.lastname: Cachia
authors.forename: P J
authors.initials: PJ
authors.lastname: Flamion
authors.forename: J P
authors.initials: JP
authors.lastname: Schreiber
mesh_terms: D001426:Bacterial Proteins / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods; D004926:Escherichia coli / Q000737:chemistry; D012269:Ribosomal Proteins / Q000302:isolation & purification*
chemical_list: D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C040469:ribosomal protein S30