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NCS-constrained exhaustive search using oligomeric models

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NCS-constrained exhaustive search using oligomeric models. / Isupov, Michail N.; Lebedev, Andrey A.

In: Acta crystallographica section d-Biological crystallography, Vol. 64, No. 1, 04.01.2008, p. 90-98.

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Harvard

Isupov, MN & Lebedev, AA 2008, 'NCS-constrained exhaustive search using oligomeric models', Acta crystallographica section d-Biological crystallography, vol. 64, no. 1, pp. 90-98. https://doi.org/10.1107/S0907444907053802

APA

Isupov, M. N., & Lebedev, A. A. (2008). NCS-constrained exhaustive search using oligomeric models. Acta crystallographica section d-Biological crystallography, 64(1), 90-98. https://doi.org/10.1107/S0907444907053802

Vancouver

Isupov MN, Lebedev AA. NCS-constrained exhaustive search using oligomeric models. Acta crystallographica section d-Biological crystallography. 2008 Jan 4;64(1):90-98. https://doi.org/10.1107/S0907444907053802

Author

Isupov, Michail N. ; Lebedev, Andrey A. / NCS-constrained exhaustive search using oligomeric models. In: Acta crystallographica section d-Biological crystallography. 2008 ; Vol. 64, No. 1. pp. 90-98.

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@article{ab065969dcc148cfb2c8f1909d8d0602,
title = "NCS-constrained exhaustive search using oligomeric models",
abstract = "The efficiency of the cross-rotation function step of molecular replacement (MR) is intrinsically limited as it uses only a fraction of the Patterson vectors. Along with general techniques extending the boundaries of the method, there are approaches that utilize specific features of a given structure. In special cases, where the directions of noncrystallographic symmetry axes can be unambiguously derived from the self-rotation function and the structure of the homologue protein is available in a related oligomeric state, the cross-rotation function step of MR can be omitted. In such cases, a small number of yet unknown parameters defining the orientation of the oligomer and/or its internal organization can be optimized using an exhaustive search. Three difficult MR cases are reported in which these parameters were determined and the oligomer was positioned according to the maximal value of the correlation coefficient in a series of translation searches.",
keywords = "NON-CRYSTALLOGRAPHIC SYMMETRY, X-RAY-DIFFRACTION, MOLECULAR-REPLACEMENT, ANGSTROM RESOLUTION, CRYSTAL-STRUCTURE, PSEUDOMONAS-PUTIDA, 3-DIMENSIONAL STRUCTURE, BACTERIAL LUCIFERASE, PROTEIN, CRYSTALLIZATION",
author = "Isupov, {Michail N.} and Lebedev, {Andrey A.}",
year = "2008",
month = "1",
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doi = "10.1107/S0907444907053802",
language = "English",
volume = "64",
pages = "90--98",
journal = "Acta crystallographica section d-Biological crystallography",
issn = "0907-4449",
publisher = "International Union of Crystallography",
number = "1",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - NCS-constrained exhaustive search using oligomeric models

AU - Isupov, Michail N.

AU - Lebedev, Andrey A.

PY - 2008/1/4

Y1 - 2008/1/4

N2 - The efficiency of the cross-rotation function step of molecular replacement (MR) is intrinsically limited as it uses only a fraction of the Patterson vectors. Along with general techniques extending the boundaries of the method, there are approaches that utilize specific features of a given structure. In special cases, where the directions of noncrystallographic symmetry axes can be unambiguously derived from the self-rotation function and the structure of the homologue protein is available in a related oligomeric state, the cross-rotation function step of MR can be omitted. In such cases, a small number of yet unknown parameters defining the orientation of the oligomer and/or its internal organization can be optimized using an exhaustive search. Three difficult MR cases are reported in which these parameters were determined and the oligomer was positioned according to the maximal value of the correlation coefficient in a series of translation searches.

AB - The efficiency of the cross-rotation function step of molecular replacement (MR) is intrinsically limited as it uses only a fraction of the Patterson vectors. Along with general techniques extending the boundaries of the method, there are approaches that utilize specific features of a given structure. In special cases, where the directions of noncrystallographic symmetry axes can be unambiguously derived from the self-rotation function and the structure of the homologue protein is available in a related oligomeric state, the cross-rotation function step of MR can be omitted. In such cases, a small number of yet unknown parameters defining the orientation of the oligomer and/or its internal organization can be optimized using an exhaustive search. Three difficult MR cases are reported in which these parameters were determined and the oligomer was positioned according to the maximal value of the correlation coefficient in a series of translation searches.

KW - NON-CRYSTALLOGRAPHIC SYMMETRY

KW - X-RAY-DIFFRACTION

KW - MOLECULAR-REPLACEMENT

KW - ANGSTROM RESOLUTION

KW - CRYSTAL-STRUCTURE

KW - PSEUDOMONAS-PUTIDA

KW - 3-DIMENSIONAL STRUCTURE

KW - BACTERIAL LUCIFERASE

KW - PROTEIN

KW - CRYSTALLIZATION

UR - http://www.scopus.com/inward/record.url?scp=37349122514&partnerID=8YFLogxK

U2 - 10.1107/S0907444907053802

DO - 10.1107/S0907444907053802

M3 - Article

VL - 64

SP - 90

EP - 98

JO - Acta crystallographica section d-Biological crystallography

JF - Acta crystallographica section d-Biological crystallography

SN - 0907-4449

IS - 1

ER -