Neutron macromolecular crystallography

被引：85

作者：

Blakeley, M. P. ^{[1
]}

机构：

[1] Inst Max Von Laue Paul Langevin, Large Scale Struct Grp, F-38042 Grenoble 9, France

来源：

CRYSTALLOGRAPHY REVIEWS | 2009年 / 15卷 / 03期

关键词：

bound solvent; deuterium; deuteron; hydrogen; joint X-ray and neutron refinement; macromolecule; neutron image plate; nucleic acid; perdeuteration; proton; protonation-state; protein; quasi-Laue; reactor source; single crystal; spallation source; time-of-flight Laue; D-XYLOSE ISOMERASE; OF-FLIGHT NEUTRON; HIGH-RESOLUTION NEUTRON; X-RAY-DIFFRACTION; HUMAN ALDOSE REDUCTASE; ASPARTIC PROTEINASE ENDOTHIAPEPSIN; VITAMIN-B12 COENZYME CRYSTALS; HYDROGEN-BONDING GEOMETRIES; PHOTOACTIVE YELLOW PROTEIN; IMAGE-PLATE DETECTORS;

D O I：

10.1080/08893110902965003

中图分类号：

O7 [晶体学];

学科分类号：

070301 [无机化学];

摘要：

Neutron crystallography allows direct determination of the proton and deuteron positions of a macromolecule and its bound solvent. Key advances in neutron macromolecular crystallography have led to an expanding field addressing larger and more complex problems. In particular, improvements in neutron instrumentation, detection systems, data collection methods and perdeuterated sample preparation have dramatically lowered the sample volume requirements to similar to 0.1-0.2 mm(3) and data collection times to just a few days. This trend towards the study of larger systems using smaller samples is set to continue with instrumentation being built at new sources and upgrades being made to existing instrumentation. These developments make it desirable to summarize the current status of neutron macromolecular crystallography and offer some perspectives for the future. In addition, using examples of the neutron structures determined so far, I will present the wealth of information that can be gained from such studies and illustrate how this can be vital towards understanding macromolecular function and behaviour.

引用

页码：157 / 218

页数：62

共 210 条

[1]

ADACHI M, P NATL ACAD SCI US, V106, P4641

[2]

Recent developments in the PHENIX software for automated crystallographic structure determination [J].

Adams, PD ;

Gopal, K ;

Grosse-Kunstleve, RW ;

Hung, LW ;

Ioerger, TR ;

McCoy, AJ ;

Moriarty, NW ;

Pai, RK ;

Read, RJ ;

Romo, TD ;

Sacchettin, JC ;

Sauter, NK ;

Storoni, LC ;

Terwilligerf, TC .

JOURNAL OF SYNCHROTRON RADIATION, 2004, 11 :53-55

[3]

Afonine P.V., 2005, CCP4 Newsl, V42, P8

[4]

The determination of protonation states in proteins [J].

Ahmed, H. U. ;

Blakeley, M. P. ;

Cianci, M. ;

Cruickshank, D. W. J. ;

Hubbard, J. A. ;

Helliwell, J. R. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2007, 63 :906-922

[5]

ALBERI JL, 1976, BROOKHAVEN SYM BIOL, V27, P24

[6]

[Anonymous], [No title captured]

[7]

Complicated water orientations in the minor groove of the B-DNA decamer d(CCATTAATGG)2 observed by neutron diffraction measurements [J].

Arai, S ;

Chatake, T ;

Ohhara, T ;

Kurihara, K ;

Tanaka, I ;

Suzuki, N ;

Fujimoto, Z ;

Mizuno, H ;

Niimura, N .

NUCLEIC ACIDS RESEARCH, 2005, 33 (09) :3017-3024

[8]

Crystallization of a large single crystal of a B-DNA decamer for a neutron diffraction experiment by the phase-diagram technique [J].

Arai, S ;

Chatake, T ;

Minezaki, Y ;

Niimura, N .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2002, 58 :151-153

[9]

A comparison of refined X-ray structures of hydrogenated and perdeuterated rat γE-crystallin in H2O and D2O [J].

Artero, JB ;

Härtlein, M ;

McSweeney, S ;

Timmins, P .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2005, 61 :1541-1549

[10]

LSCALE -: the new normalization, scaling and absorption correction program in the Daresbury Laue software suite [J].

Arzt, S ;

Campbell, JW ;

Harding, MM ;

Hao, Q ;

Helliwell, JR .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1999, 32 :554-562

← 1 2 3 4 5 6 7 8 9 10 →