Use of Dual Polarization Interferometry as a Diagnostic Tool for Protein Crystallization

被引:14
作者
Boudjemline, Attia [1 ]
Saridakis, Emmanuel [2 ]
Swann, Marcus J. [1 ]
Govada, Lata [3 ]
Mavridis, Irene M. [2 ]
Chayen, Naomi E. [3 ]
机构
[1] Farfield Grp Ltd, Manchester M90 3DQ, Lancs, England
[2] Natl Ctr Sci Res Demokritos, Inst Phys Chem, Athens 15310, Greece
[3] Univ London Imperial Coll Sci Technol & Med, Fac Med, Dept Surg & Canc, London SW7 2AZ, England
关键词
SWEET PROTEIN; THAUMATIN-I; CRYSTAL; SOLUBILITY; LYSOZYME; GROWTH;
D O I
10.1021/ac2017844
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
The use of dual polarization interferometry (DPI) as a tool for probing the different possible outcomes of protein crystallization experiments is described. DPI is a surface analytical technique used for the characterization of structure and interactions of molecular layers on an optical waveguide surface for a wide range of applications, including protein-protein interactions and conformational changes The application of this technique provides a "signature" of crystallization events, thus predicting if there will be protein crystal formation, amorphous precipitate, or clear solution.. The technique was demonstrated on a number of model proteins, and it also produced meaningful results in the case of two problematic target proteins DPI in conjunction with a dialysis, setup, allows changes in the protein solution above the waveguide surface to be monitored. simultaneously with continuous control of its precipitant content DPI has the potential to be used as a powerful method for discovering crystallization conditions, for obtaining information on the crystallization process, and as an aid in crystal optimization. It has also provided what is, to the best of our knowledge, the most direct observation to date of salting in behavior in a protein salt solution.
引用
收藏
页码:7881 / 7887
页数:7
相关论文
共 20 条
[1]   THE GROWTH OF LARGE SINGLE-CRYSTALS OF LYSOZYME [J].
ATAKA, M ;
TANAKA, S .
BIOPOLYMERS, 1986, 25 (02) :337-350
[2]   Early stages of protein crystallization as revealed by emerging optical waveguide technology [J].
Boudjemline, Attia ;
Clarke, David T. ;
Freeman, Neville J. ;
Nicholson, James M. ;
Jones, Gareth R. .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 2008, 41 :523-530
[3]   THE SOLUBILITY OF THE TETRAGONAL FORM OF HEN EGG-WHITE LYSOZYME FROM PH 4.0 TO 5.4 [J].
CACIOPPO, E ;
PUSEY, ML .
JOURNAL OF CRYSTAL GROWTH, 1991, 114 (03) :286-292
[4]   Protein crystallization: from purified protein to diffraction-quality crystal [J].
Chayen, Naomi E. ;
Saridakis, Emmanuel .
NATURE METHODS, 2008, 5 (02) :147-153
[5]   Porous silicon: an effective nucleation-inducing material for protein crystallization [J].
Chayen, NE ;
Saridakis, E ;
El-Bahar, R ;
Nemirovsky, Y .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 312 (04) :591-595
[6]   A new quantitative optical biosensor for protein characterisation [J].
Cross, GH ;
Reeves, AA ;
Brand, S ;
Popplewell, JF ;
Peel, LL ;
Swann, MJ ;
Freeman, NJ .
BIOSENSORS & BIOELECTRONICS, 2003, 19 (04) :383-390
[7]   Young's fringes from vertically integrated slab waveguides: Applications to humidity sensing [J].
Cross, GH ;
Ren, YT ;
Freeman, NJ .
JOURNAL OF APPLIED PHYSICS, 1999, 86 (11) :6483-6488
[8]  
CROSS GH, 2007, HDB BIOSENSORS BIOCH, V1, P549
[9]  
CUDNEY B, 1994, ACTA CRYSTALLOGR D, V50, P414, DOI 10.1107/S0907444994002660
[10]  
DEVOS AM, 1985, P NATL ACAD SCI USA, V82, P1406