Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10844050 | Protein Expression and Purification | 2005 | 11 Pages |
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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Biochemistry
Authors
Jörg Peters, Torsten Minuth, Werner Schröder,