Microtubule structure at 8 Å resolution

Huilin Li; David J. DeRosier; William V. Nicholson; Eva Nogales; Kenneth H. Downing

doi:10.1016/S0969-2126(02)00827-4

Microtubule structure at 8 Å resolution

Huilin Li
, David J. DeRosier
, William V. Nicholson
, Eva Nogales
, Kenneth H. Downing

Research output: Contribution to journal › Article › peer-review

360 Citations (Scopus)

Abstract

We have obtained a 3D reconstruction of intact microtubules, using cryoelectron microscopy and image processing, at a resolution of about 8 Å, sufficient to resolve much of the secondary structure. The level of detail in the map allows docking of the tubulin structure previously determined by electron crystallography, with very strong constraints, providing several important insights not previously available through docking tubulin into lower-resolution maps. This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.

Original language	English
Pages (from-to)	1317-1328
Number of pages	12
Journal	Structure
Volume	10
Issue number	10
DOIs	https://doi.org/10.1016/S0969-2126(02)00827-4
Publication status	Published - 2002

Keywords

TUBULIN
microtubules
electron crystallography
Protein structure
dynamic instability

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10.1016/S0969-2126(02)00827-4

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@article{f1487acf96c64d34aa8948712d094d59,

title = "Microtubule structure at 8 {\AA} resolution",

abstract = "We have obtained a 3D reconstruction of intact microtubules, using cryoelectron microscopy and image processing, at a resolution of about 8 {\AA}, sufficient to resolve much of the secondary structure. The level of detail in the map allows docking of the tubulin structure previously determined by electron crystallography, with very strong constraints, providing several important insights not previously available through docking tubulin into lower-resolution maps. This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.",

keywords = "TUBULIN, microtubules, electron crystallography, Protein structure, dynamic instability",

author = "Huilin Li and DeRosier, \{David J.\} and Nicholson, \{William V.\} and Eva Nogales and Downing, \{Kenneth H.\}",

year = "2002",

doi = "10.1016/S0969-2126(02)00827-4",

language = "English",

volume = "10",

pages = "1317--1328",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "10",

}

TY - JOUR

T1 - Microtubule structure at 8 Å resolution

AU - Li, Huilin

AU - DeRosier, David J.

AU - Nicholson, William V.

AU - Nogales, Eva

AU - Downing, Kenneth H.

PY - 2002

Y1 - 2002

N2 - We have obtained a 3D reconstruction of intact microtubules, using cryoelectron microscopy and image processing, at a resolution of about 8 Å, sufficient to resolve much of the secondary structure. The level of detail in the map allows docking of the tubulin structure previously determined by electron crystallography, with very strong constraints, providing several important insights not previously available through docking tubulin into lower-resolution maps. This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.

AB - We have obtained a 3D reconstruction of intact microtubules, using cryoelectron microscopy and image processing, at a resolution of about 8 Å, sufficient to resolve much of the secondary structure. The level of detail in the map allows docking of the tubulin structure previously determined by electron crystallography, with very strong constraints, providing several important insights not previously available through docking tubulin into lower-resolution maps. This work provides an improved picture of the interactions between adjacent protofilaments, which are responsible for microtubule stability, and also suggests that some structural features are different in microtubules from those in the zinc sheets with which the tubulin structure was determined.

KW - TUBULIN

KW - microtubules

KW - electron crystallography

KW - Protein structure

KW - dynamic instability

UR - https://www.scopus.com/pages/publications/0036774026

U2 - 10.1016/S0969-2126(02)00827-4

DO - 10.1016/S0969-2126(02)00827-4

M3 - Article

SN - 0969-2126

VL - 10

SP - 1317

EP - 1328

JO - Structure

JF - Structure

IS - 10

ER -

Microtubule structure at 8 Å resolution

Abstract

Keywords

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Microtubule structure at 8 Å resolution

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