Peters Jörg, Minuth Torsten, Schröder Werner
Bayer HealthCare AG, Friedrich-Ebert-Str. 217, D-42096 Wuppertal, Germany.
Protein Expr Purif. 2005 Jan;39(1):43-53. doi: 10.1016/j.pep.2004.09.011.
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.
新蛋白质结晶条件的确定仍被视为一项繁琐的反复试验工作，尤其是当结晶步骤必须满足特定纯化过程的要求时。就寻找与重组抑肽酶变体纯化过程相兼容的新结晶条件的能力而言，对传统的筛选试剂盒方法和多因素方法进行了比较。总体而言，多因素方法的效率高出10倍。新的结晶条件被放大并作为一个大量储存步骤应用于纯化过程。对由此过程获得的抑肽酶变体进行了全面的生化表征。
