Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches

Wah Chiu; Matthew L. Baker; Wen Jiang; Z. Hong Zhou

doi:10.1016/S0959-440X(02)00319-6

Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches

Wah Chiu
, Matthew L. Baker
, Wen Jiang
, Z. Hong Zhou

Research output: Contribution to journal › Review article › peer-review

40 Scopus citations

Abstract

Intermediate-resolution (7-9 Å) structures of large macromolecular complexes can be obtained by electron cryomicroscopy. This structural information, combined with bioinformatics data for the individual protein components or domains, can lead to a fold model for the entire complex. Such approaches have been demonstrated with the 6.8 Å structure of the rice dwarf virus to derive models for the major capsid shell proteins.

Original language	English (US)
Pages (from-to)	263-269
Number of pages	7
Journal	Current Opinion in Structural Biology
Volume	12
Issue number	2
DOIs	https://doi.org/10.1016/S0959-440X(02)00319-6
State	Published - Apr 1 2002

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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10.1016/S0959-440X(02)00319-6

Cite this

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title = "Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches",

abstract = "Intermediate-resolution (7-9 {\AA}) structures of large macromolecular complexes can be obtained by electron cryomicroscopy. This structural information, combined with bioinformatics data for the individual protein components or domains, can lead to a fold model for the entire complex. Such approaches have been demonstrated with the 6.8 {\AA} structure of the rice dwarf virus to derive models for the major capsid shell proteins.",

author = "Wah Chiu and Baker, \{Matthew L.\} and Wen Jiang and Zhou, \{Z. Hong\}",

year = "2002",

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AU - Chiu, Wah

AU - Baker, Matthew L.

AU - Jiang, Wen

AU - Zhou, Z. Hong

PY - 2002/4/1

Y1 - 2002/4/1

N2 - Intermediate-resolution (7-9 Å) structures of large macromolecular complexes can be obtained by electron cryomicroscopy. This structural information, combined with bioinformatics data for the individual protein components or domains, can lead to a fold model for the entire complex. Such approaches have been demonstrated with the 6.8 Å structure of the rice dwarf virus to derive models for the major capsid shell proteins.

AB - Intermediate-resolution (7-9 Å) structures of large macromolecular complexes can be obtained by electron cryomicroscopy. This structural information, combined with bioinformatics data for the individual protein components or domains, can lead to a fold model for the entire complex. Such approaches have been demonstrated with the 6.8 Å structure of the rice dwarf virus to derive models for the major capsid shell proteins.

UR - https://www.scopus.com/pages/publications/0036535896

UR - https://www.scopus.com/pages/publications/0036535896#tab=citedBy

U2 - 10.1016/S0959-440X(02)00319-6

DO - 10.1016/S0959-440X(02)00319-6

M3 - Review article

C2 - 11959506

AN - SCOPUS:0036535896

SN - 0959-440X

VL - 12

SP - 263

EP - 269

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

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ER -

Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches

Abstract

All Science Journal Classification (ASJC) codes

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