The factors during protein crystallization: A review
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RYSTAL GROWTH
The Factors during Protein Crystallization: A Review1 X. X. Li, X. D. Xu, Y. Y. Dan, and M. L. Zhang College of Materials Science and Chemical Engineering, Harbin Engineering University, Harbin, China e-mail: [email protected] Received August 2, 2007
Abstract—Many factors have effects on crystallization. The major influencing factors during protein crystallization are summarized in this paper. Recommendations are made about the basic process of crystallization and the analysis of the thermodynamic effects on crystallization, and the dynamics factors effecting crystallization during an equilibrium process are discussed. The advantages of ionic liquid in various chemical processes, especially in the field of biochemistry, are emphasized, and some tentative conclusions are made about future short-term trends. PACS numbers: 81.10.Dn, 81.10-h DOI: 10.1134/S1063774508070286
INTRODUCTION The crystallization of protein has been intensively studied in the last three decades [1–3]. Although Feher [4] and McPherson [5] illuminated its principle and established some basic methods 20 years ago, the theory about how to influence the procedure of crystallization remains unclear. In fact, the crystallization of protein is much more difficult than that of little molecular compounds owing to proteins' variety of molecular weights, shapes, aggregate states, and surface features that change with pH and temperature. Currently, the situation of protein crystallization is an empirical search. To some extent, it relies on opportunity. However, through constant efforts, a considerable amount of success has been achieved. Because the function of the proteins and nucleohistones is mostly a reflection of their unique 3D structures, it is necessary to measure and research them in order to well understand how the molecules work in an organism. Otherwise, on the basis of the knowledge in this content, we could develop several functional molecules via different applications. X-ray diffraction is a reliable method for analysis of the structures of biological macromolecules. Although there are many other ways to acquire the structure of biomacromolecules, the data that can be set out are so limited that it is difficult to calculate full and clear information in most cases. The measurement of the protein crystal is especially suitable for the study of the steric structure of protein via X-ray diffraction and it will be the most important method in subsequent years. The main objective of the study on protein crystallization is to acquire a perfect crystal. This goal requires 1The
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unambiguous intension of reflections from lattice planes, at least 1–1.5 Å spacing [6], and the production of a single crystal [7]. From the X-ray diffraction pattern of a single crystal, we can work out the lattice parameters, the crystal structure, and other useful information. Accordingly, the crystal’s 3D structure, which has attracted special attention from proteomics researchers, may be found. Current
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