Implementation of a crystallization step into the purification process of a recombinant protein
Related Experiment Video
Updated: Aug 20, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Jörg Peters1, Torsten Minuth, Werner Schröder
1Bayer HealthCare AG, Friedrich-Ebert-Str. 217, D-42096 Wuppertal, Germany. JOERG.PETERS@bayerhealthcare.com
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.
Related Concept Videos
Recrystallization: Solid–Solution Equilibria
Downstream Processing
Crystal Growth: Principles of Crystallization
Initiating crystallization involves manipulating the concentration of the solute and the temperature of the solution. Since crystal growth occurs when the ratio of concentration and solubility of the solute in the solvent – the...
Immunoprecipitation
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Upstream Processing

