Combining X-ray crystallography and electron microscopy

Michael G. Rossmann; Marc C. Morais; Petr G. Leiman; Wei Zhang

doi:10.1016/j.str.2005.01.005

Combining X-ray crystallography and electron microscopy

Michael G. Rossmann, Marc C. Morais, Petr G. Leiman, Wei Zhang

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

105 Scopus citations

Abstract

The combination of cryo-electron microscopy to study large biological assemblies at low resolution with crystallography to determine near atomic structures of assembly fragments is quickly expanding the horizon of structural biology. This technique can be used to advantage in the study of large structures that cannot be crystallized, to follow dynamic processes, and to "purify" samples by visual selection of particles. Factors affecting the quality of cryo-electron microscopy maps and limits of accuracy in fitting known structural fragments are discussed.

Original language	English (US)
Pages (from-to)	355-362
Number of pages	8
Journal	Structure
Volume	13
Issue number	3
DOIs	https://doi.org/10.1016/j.str.2005.01.005
State	Published - Mar 2005
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2005.01.005

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title = "Combining X-ray crystallography and electron microscopy",

abstract = "The combination of cryo-electron microscopy to study large biological assemblies at low resolution with crystallography to determine near atomic structures of assembly fragments is quickly expanding the horizon of structural biology. This technique can be used to advantage in the study of large structures that cannot be crystallized, to follow dynamic processes, and to {"}purify{"} samples by visual selection of particles. Factors affecting the quality of cryo-electron microscopy maps and limits of accuracy in fitting known structural fragments are discussed.",

author = "Rossmann, {Michael G.} and Morais, {Marc C.} and Leiman, {Petr G.} and Wei Zhang",

note = "Funding Information: The structural examples given here are derived from a large number of collaborators, postdoctoral researchers, graduate students, and technical assistants who are recognized by virtue of the quoted references. Similarly, the sources of financial support are numerous, but successive National Institutes of Health grants have supported work on the eukaryotic viruses, while successive National Science Foundation grants and a Human Frontier Science Program grant have supported the bacteriophage studies. We thank Cheryl Towell for her help in preparing this manuscript.",

year = "2005",

month = mar,

doi = "10.1016/j.str.2005.01.005",

language = "English (US)",

volume = "13",

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journal = "Structure",

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publisher = "Cell Press",

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T1 - Combining X-ray crystallography and electron microscopy

AU - Rossmann, Michael G.

AU - Morais, Marc C.

AU - Leiman, Petr G.

AU - Zhang, Wei

N1 - Funding Information: The structural examples given here are derived from a large number of collaborators, postdoctoral researchers, graduate students, and technical assistants who are recognized by virtue of the quoted references. Similarly, the sources of financial support are numerous, but successive National Institutes of Health grants have supported work on the eukaryotic viruses, while successive National Science Foundation grants and a Human Frontier Science Program grant have supported the bacteriophage studies. We thank Cheryl Towell for her help in preparing this manuscript.

PY - 2005/3

Y1 - 2005/3

N2 - The combination of cryo-electron microscopy to study large biological assemblies at low resolution with crystallography to determine near atomic structures of assembly fragments is quickly expanding the horizon of structural biology. This technique can be used to advantage in the study of large structures that cannot be crystallized, to follow dynamic processes, and to "purify" samples by visual selection of particles. Factors affecting the quality of cryo-electron microscopy maps and limits of accuracy in fitting known structural fragments are discussed.

AB - The combination of cryo-electron microscopy to study large biological assemblies at low resolution with crystallography to determine near atomic structures of assembly fragments is quickly expanding the horizon of structural biology. This technique can be used to advantage in the study of large structures that cannot be crystallized, to follow dynamic processes, and to "purify" samples by visual selection of particles. Factors affecting the quality of cryo-electron microscopy maps and limits of accuracy in fitting known structural fragments are discussed.

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DO - 10.1016/j.str.2005.01.005

M3 - Review article

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VL - 13

SP - 355

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JO - Structure

JF - Structure

IS - 3

ER -

Combining X-ray crystallography and electron microscopy

Abstract

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