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Uncertainties in crystallization of hen‐egg white lysozyme: reproducibility issue
Author(s) -
Yin DaChuan,
Wakayama Nobuko I.,
Lu HuiMeng,
Ye YaJing,
Li HaiSheng,
Luo HuiMin,
Inatomi Yuko
Publication year - 2008
Publication title -
crystal research and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.377
H-Index - 64
eISSN - 1521-4079
pISSN - 0232-1300
DOI - 10.1002/crat.200710998
Subject(s) - crystallization , lysozyme , orthorhombic crystal system , tetragonal crystal system , nucleation , protein crystallization , isothermal process , reproducibility , crystallography , materials science , chemistry , chemical engineering , chromatography , thermodynamics , crystal structure , biochemistry , physics , organic chemistry , engineering
The reproducibility of biomacromolecular crystallization (tetragonal and orthorhombic lysozyme crystals) was studied by monitoring the evolution of protein concentration during the crystallization process using Mach‐Zehnder interferometer. It was found that formation of both tetragonal and orthorhombic crystals exhibited poor reproducibility. When the crystallization occurred under isothermal conditions, the protein concentration in the solution varied differently in different experiments under identical conditions (for both types of crystals). Moreover, in the case of orthorhombic lysozyme crystallization (under either isothermal or thermal gradient conditions), it is clear that the crystals could not be always readily formed. When formation of tetragonal lysozyme crystals was conducted at a temperature gradient condition, however, the evolution of concentration was reproducible. The phenomena found in this study revealed that biomacromolecular crystallization can be uncertain, which is probably caused by the process of nucleation. Such uncertainties will be harmful for the efforts of screening crystallization conditions for biomacromolecules. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)