Incorporation of impurity to a tetragonal lysozyme crystal

• Published in: Journal of crystal growth Vol. 196; no. 2; pp. 285 - 290
• Main Authors: Kurihara, Kazuo, Miyashita, Satoru, Sazaki, Gen, Nakada, Toshitaka, Durbin, Stephen D, Komatsu, Hiroshi, Ohba, Tetsuhiko, Ohki, Kazuo
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Amsterdam Elsevier B.V 01-01-1999; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Crystal growth; Fluorescence; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Impurity; Incorporation; Lysozyme; Ovalbumin; Proteins; Crystal growth; Ovalbumin; Incorporation; Impurity; Fluorescence; 61.72.S; 87.15; 81.10.A; 36.20; Lysozyme; Enzyme; Glycosidases; Crystallization; Hydrolases; O-Glycosidases; Protein
• ISSN: 0022-0248; 1873-5002
• DOI: 10.1016/S0022-0248(98)00872-0

Concentration of a phosphor-labeled impurity (ovalbumin) incorporated into protein (hen egg white lysozyme) crystals during growth was measured by fluorescence.This technique enabled us to measure the local impurity concentration in a crystal quantitatively. Impurity concentration increased with growth rate, which could not be explained by two conventional models (equilibrium adsorption model and Burton–Prim–Slichter model); a modified model is proposed. Impurity concentration also increased with the pH of the solution. This result is discussed considering the electrostatic interaction between the impurity and the crystallizing species.