Rational protein crystallization by mutational surface engineering

被引:217
作者
Derewenda, ZS [1 ]
机构
[1] Univ Virginia, Sch Med, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA
关键词
D O I
10.1016/j.str.2004.03.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein crystallization constitutes a limiting step in structure determination by X-ray diffraction. Even if single crystals are available, inadequate physical quality may seriously limit the resolution of the available data and consequently the accuracy of the atomic model. Recent studies show that targeted mutagenesis of surface patches containing residues with large flexible side chains and their replacement with smaller amino acids lead to effective preparation of X-ray quality crystals of proteins otherwise recalcitrant to crystallization. Furthermore, this technique can also be used to obtain crystals of superior quality as compared to those grown for the wild-type protein, sometimes increasing the effective resolution by as much as 1 A or more. Several recent examples of this new methodology suggest that the method has the potential to become a routine tool in protein crystallography.
引用
收藏
页码:529 / 535
页数:7
相关论文
共 28 条
[1]   Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins [J].
Avbelj, F ;
Fele, L .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 279 (03) :665-684
[2]   Controlling IGF-receptor function: A possible strategy for tumor therapy [J].
Baserga, R .
TRENDS IN BIOTECHNOLOGY, 1996, 14 (05) :150-152
[3]   Measures of residue density in protein structures [J].
Baud, F ;
Karlin, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (22) :12494-12499
[4]   THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].
BRAIG, K ;
OTWINOWSKI, Z ;
HEGDE, R ;
BOISVERT, DC ;
JOACHIMIAK, A ;
HORWICH, AL ;
SIGLER, PB .
NATURE, 1994, 371 (6498) :578-586
[5]  
Campbell J W, 1972, Cold Spring Harb Symp Quant Biol, V36, P165
[6]   Prediction of tight turns and their types in proteins [J].
Chou, KC .
ANALYTICAL BIOCHEMISTRY, 2000, 286 (01) :1-16
[7]   The impact of Lys→Arg surface mutations on the crystallization of the globular domain of RhoGDI [J].
Czepas, J ;
Devedjiev, Y ;
Krowarsch, D ;
Derewenda, U ;
Otlewski, J ;
Derewenda, ZS .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2004, 60 :275-280
[8]   The protein as a variable in protein crystallization [J].
Dale, GE ;
Oefner, C ;
D'Arcy, A .
JOURNAL OF STRUCTURAL BIOLOGY, 2003, 142 (01) :88-97
[9]  
Dasgupta S, 1997, PROTEINS, V28, P494, DOI 10.1002/(SICI)1097-0134(199708)28:4<494::AID-PROT4>3.0.CO
[10]  
2-A