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A new approach to the crystallization of proteins
Author(s) -
Gulewicz K.,
Adamiak D.,
Sprinzl M.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81019-x
Subject(s) - crystallization , protein crystallization , lysozyme , ionic strength , chemistry , adsorption , chromatography , crystallography , chymotrypsin , ionic bonding , crystal (programming language) , matrix (chemical analysis) , chemical engineering , biochemistry , enzyme , organic chemistry , trypsin , ion , programming language , aqueous solution , computer science , engineering
A new method for the crystallization of proteins was developed. Saturated solutions of a protein for crystallization are prepared by chromatography of adsorbed proteins from an insoluble polysaccharide matrix using gradients with decreasing ionic strength, decreasing concentration of organic solvents or an appropriate shift in pH. Insulin, a‐chymotrypsin and lysozyme for which the X‐ray crystal structures are known, were crystallized by this method. X‐ray diffraction photographs were taken to demonstrate the quality of the crystals. In addition to this analytical application, the method may be useful for the crystallization and the simultaneous purification of larger amounts of proteins.