Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules

被引：141

作者：

Adams, Paul D. ^{[2
,3
]}

Mustyakimov, Marat ^{[1
]}

Afonine, Pavel V. ^{[2
]}

Langan, Paul ^{[1
]}

机构：

[1] Los Alamos Natl Lab, Los Alamos, NM 87545 USA

[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley, CA 94720 USA

[3] Univ Calif Berkeley, Dept Bioengn, Berkeley, CA 94720 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2009年 / 65卷

关键词：

MAXIMUM-LIKELIHOOD; STRUCTURE REFINEMENT; MOLECULAR-DYNAMICS; DIFFRACTION DATA; SOFTWARE;

D O I：

10.1107/S0907444909011548

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

X-ray and neutron crystallographic techniques provide complementary information on the structure and function of biological macromolecules. X-ray and neutron (XN) crystallographic data have been combined in a joint structure-refinement procedure that has been developed using recent advances in modern computational methodologies, including cross-validated maximum-likelihood target functions with gradient-based optimization and simulated annealing. The XN approach for complete (including hydrogen) macromolecular structure analysis provides more accurate and complete structures, as demonstrated for diisopropyl fluorophosphatase, photoactive yellow protein and human aldose reductase. Furthermore, this method has several practical advantages, including the easier determination of the orientation of water molecules, hydroxyl groups and some amino-acid side chains.

引用

页码：567 / 573

页数：7

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