Implementation of a crystallization step into the purification process of a recombinant protein |
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Authors: | Peters Jörg Minuth Torsten Schröder Werner |
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Affiliation: | Bayer HealthCare AG, Friedrich-Ebert-Str. 217, D-42096 Wuppertal, Germany. JOERG.PETERS@bayerhealthcare.com |
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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. |
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