On the molecular-replacement problem in the presence of merohedral twinning: structure of the N-terminal half-molecule of human lactoferrin

被引:24
作者
Breyer, WA [1 ]
Kingston, RL [1 ]
Anderson, BF [1 ]
Baker, EN [1 ]
机构
[1] Massey Univ, Dept Biochem, Palmerston North, New Zealand
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1999年 / 55卷
关键词
D O I
10.1107/S0907444998009640
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The structure of a hemihedrally twinned protein crystal with two molecules in the asymmetric unit was solved by molecular replacement. The protein, a site-specific mutant of the N-terminal half-molecule of human lactoferrin, is able to undergo an internal rigid-body domain motion. Therefore, determining the structure required the independent positioning of four protein domains The molecular-replacement solutions were obtained using a conventional real-space rotation function, and a translation function based on the linear correlation coefficient. Once the molecules were positioned, it was necessary to assign them to the appropriate twin domain. Several methods for doing this are described, one of which leads to a determination of the volume of each twin domain. In the appendix to the paper we discuss the interpretation of the self-rotation function in the presence of merohedral twinning.
引用
收藏
页码:129 / 138
页数:10
相关论文
共 43 条
[11]   ACCURATE BOND AND ANGLE PARAMETERS FOR X-RAY PROTEIN-STRUCTURE REFINEMENT [J].
ENGH, RA ;
HUBER, R .
ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :392-400
[12]   Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: Crystal structures of R121S and R121E mutants [J].
Faber, HR ;
Baker, CJ ;
Day, CL ;
Tweedie, JW ;
Baker, EN .
BIOCHEMISTRY, 1996, 35 (46) :14473-14479
[13]   A MUTANT T4 LYSOZYME DISPLAYS 5 DIFFERENT CRYSTAL CONFORMATIONS [J].
FABER, HR ;
MATTHEWS, BW .
NATURE, 1990, 348 (6298) :263-266
[14]   EXPERIENCES WITH A NEW TRANSLATION-FUNCTION PROGRAM [J].
FUJINAGA, M ;
READ, RJ .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1987, 20 :517-521
[15]   DOMAIN CLOSURE IN LACTOFERRIN - 2 HINGES PRODUCE A SEE-SAW MOTION BETWEEN ALTERNATIVE CLOSE-PACKED INTERFACES [J].
GERSTEIN, M ;
ANDERSON, BF ;
NORRIS, GE ;
BAKER, EN ;
LESK, AM ;
CHOTHIA, C .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 234 (02) :357-372
[16]  
GIACOVAZZO C, 1992, FUNDAMENTALS CRYSTAL, V232, P6184
[17]   DETERMINATION OF HEMIHEDRAL TWINNING AND INITIAL STRUCTURAL-ANALYSIS OF CRYSTALS OF THE PROCARBOXYPEPTIDASE-A TERNARY COMPLEX [J].
GOMISRUTH, FX ;
FITA, I ;
KIEFERSAUER, R ;
HUBER, R ;
AVILES, FX ;
NAVAZA, J .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1995, 51 :819-823
[19]   Detwinning of hemihedrally twinned crystals by the least-squares method and its application to a crystal of hydroxylamine oxioreductase from Nitrosomanas europaea [J].
Igarashi, N ;
Moriyama, H ;
Mikami, T ;
Tanaka, N .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1997, 30 :362-367
[20]   ON STRUCTURE REFINEMENT USING DATA FROM A TWINNED CRYSTAL [J].
JAMESON, GB .
ACTA CRYSTALLOGRAPHICA SECTION A, 1982, 38 (NOV) :817-820