A high-performance neutron diffractometer for biological crystallography (BIX-3)

被引:71
作者
Tanaka, I [1 ]
Kurihara, K [1 ]
Chatake, T [1 ]
Niimura, N [1 ]
机构
[1] JAERI, Adv Sci Res Ctr, Tokai, Ibaraki 3191195, Japan
关键词
D O I
10.1107/S0021889801017745
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A high-performance neutron diffractometer for biological crystallography (BIX-3) has been constructed at JRR-3M in the Japan Atomic Energy Research Institute (JAERI) in order to determine the hydrogen-atom positions in biological macromolecules. It uses several recent technical innovations, such as a neutron imaging plate and an elastically bent silicon monochromator developed by the authors. These have made it possible to realise a compact vertical arrangement of the diffractometer. Diffraction data have been collected from the proteins rubredoxin and myoglobin in about one month, to a resolution of 1.5 Angstrom. The data were good enough to identify the hydrogen atoms with high accuracy. By adopting a crystal-step scan method for measuring Bragg diffraction intensities, the signal-to-noise ratio was much better than that of the Laue method. This shows that BIX-3 is one of the best-performing machines for neutron protein crystallography in the world today.
引用
收藏
页码:34 / 40
页数:7
相关论文
共 33 条
[1]   IMAGING PLATE ILLUMINATES MANY FIELDS [J].
AMEMIYA, Y ;
MIYAHARA, J .
NATURE, 1988, 336 (6194) :89-90
[2]   Quasi-Laue neu iron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme [J].
Bon, C ;
Lehmann, MS ;
Wilkinson, C .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1999, 55 :978-987
[3]   A LARGE IMAGE-PLATE DETECTOR FOR NEUTRONS [J].
CIPRIANI, F ;
CASTAGNA, JC ;
LEHMANN, MS ;
WILKINSON, C .
PHYSICA B, 1995, 213 :975-977
[4]   A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin [J].
Cooper, JB ;
Myles, DAA .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 :246-248
[5]  
DESIRAJU GR, 1999, WEEK HYDROGEN BOND
[6]   Direct determination of the positions of the deuterium atoms of the bound water in concanavalin A by neutron Laue crystallography [J].
Habash, J ;
Raftery, J ;
Nuttall, R ;
Price, HJ ;
Wilkinson, C ;
Kalb, AJ ;
Helliwell, JR .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2000, 56 :541-550
[7]   Gamma-ray sensitivity and shielding of a neutron imaging plate [J].
Haga, YK ;
Kumazawa, S ;
Niimura, N .
JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1999, 32 :878-882
[8]  
KURIHARA K, 2001, J PHYS SOC JPN, V70, P400
[9]   Neutron Laue diffraction studies of coenzyme cob(II)alamin [J].
Langan, P ;
Lehmann, M ;
Wilkinson, C ;
Jogl, G ;
Kratky, C .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1999, 55 :51-59
[10]  
MAEDA M, 2001, J PHYS SOC JPN, V70, P403