title: Implementation of a crystallization step into the purification process of a recombinant protein.
abstract: Identification of crystallization conditions of new proteins is still regarded as a tedious trial-and-error work, especially when the crystallization step has to meet the requirements of a given purification process. The traditional screening kit method and a multifactorial approach were compared against each other with regard to their ability to find new crystallization conditions that are compatible to the purification process of a recombinant aprotinin variant. Overall, the multifactorial approach turned out to be 10-fold more efficient. The new crystallization conditions were scaled up and implemented into the purification process as a bulk storage step. The aprotinin variant derived from this process was fully characterized biochemically.
authors.affiliation: Bayer HealthCare AG, Friedrich-Ebert-Str. 217, D-42096 Wuppertal, Germany. JOERG.PETERS@bayerhealthcare.com
authors.forename: Jörg
authors.initials: J
authors.lastname: Peters
authors.forename: Torsten
authors.initials: T
authors.lastname: Minuth
authors.forename: Werner
authors.initials: W
authors.lastname: Schröder
mesh_terms: D007611:Aprotinin / Q000031:analogs & derivatives / Q000235:genetics / Q000302:isolation & purification*; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D012965:Sodium Chloride
chemical_list: D012965:Sodium Chloride; D007611:Aprotinin