DOI: 10.1111/j.1365-2818.2012.03627.x. Pushing the resolution limits in cryo electron tomography of biological structures

Pushing the resolution limits in cryo electron tomography of biological structures

10.1111/j.1365-2818.2012.03627.x

Crossref journal-article

Wiley

Journal of Microscopy (311)

Abstract

SummaryCryo electron tomography is a three‐dimensional imaging technique that is suitable for imaging snapshots of the structural arrangements of biomolecular complexes and macromolecules, both in vitro and in the context of the cell. In terms of attainable resolution, cryo electron tomographic reconstructions now show resolvable details in the 5–10 nm range, connecting optical microscopy with molecular imaging techniques. In view of the current developments in super‐resolution light microscopy and correlative light and electron microscopy, cryo electron tomography will be increasingly important in structural biology as a tool to bridge light microscopy with molecular imaging techniques like NMR, X‐ray diffraction and single particle electron microscopy. In cell biology, one goal, often referred to as visual proteomics, is the molecular mapping of whole cells. To achieve this goal and link cryo electron tomography to these high‐resolution techniques, increasing the attainable resolution to 2–5 nm is vital. Here, we provide an overview of technical factors that limit the resolution in cryo electron tomography and discuss how during data acquisition and image processing these can be optimized to attain the highest possible resolution. Also, existing resolution measurement approaches and current technological developments that potentially increase the resolution in cryo electron tomography are discussed.

Bibliography

DIEBOLDER, CHRISTOPH. A., KOSTER, A. J., & KONING, R. I. (2012). Pushing the resolution limits in cryo electron tomography of biological structures. Journal of Microscopy, 248(1), 1â5. Portico.

Authors 3

CHRISTOPH. A. DIEBOLDER (first)
ABRAHAM J. KOSTER (additional)
ROMAN I. KONING (additional)

References 15 Referenced 49

Dates

Type	When
Created	13 years, 2 months ago (June 7, 2012, 6:49 a.m.)
Deposited	1 year, 10 months ago (Oct. 14, 2023, 6:35 p.m.)
Indexed	2 months, 1 week ago (June 9, 2025, 4:05 a.m.)
Issued	13 years, 2 months ago (June 7, 2012)
Published	13 years, 2 months ago (June 7, 2012)
Published Online	13 years, 2 months ago (June 7, 2012)
Published Print	12 years, 10 months ago (Oct. 1, 2012)

Funders 0

None

BibTeX

@article{DIEBOLDER_2012, title={Pushing the resolution limits in cryo electron tomography of biological structures}, volume={248}, ISSN={1365-2818}, url={http://dx.doi.org/10.1111/j.1365-2818.2012.03627.x}, DOI={10.1111/j.1365-2818.2012.03627.x}, number={1}, journal={Journal of Microscopy}, publisher={Wiley}, author={DIEBOLDER, CHRISTOPH. A. and KOSTER, ABRAHAM J. and KONING, ROMAN I.}, year={2012}, month=jun, pages={1–5} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        6,
        9
      ]
    ],
    "date-time": "2025-06-09T08:05:51Z",
    "timestamp": 1749456351281
  },
  "reference-count": 15,
  "publisher": "Wiley",
  "issue": "1",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2012,
            6,
            7
          ]
        ],
        "date-time": "2012-06-07T00:00:00Z",
        "timestamp": 1339027200000
      },
      "content-version": "vor",
      "delay-in-days": 0,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [
      "onlinelibrary.wiley.com"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        2012,
        10
      ]
    ]
  },
  "abstract": "<jats:title>Summary</jats:title><jats:p>Cryo electron tomography is a three\u2010dimensional imaging technique that is suitable for imaging snapshots of the structural arrangements of biomolecular complexes and macromolecules, both <jats:italic>in vitro</jats:italic> and in the context of the cell. In terms of attainable resolution, cryo electron tomographic reconstructions now show resolvable details in the 5\u201310 nm range, connecting optical microscopy with molecular imaging techniques. In view of the current developments in super\u2010resolution light microscopy and correlative light and electron microscopy, cryo electron tomography will be increasingly important in structural biology as a tool to bridge light microscopy with molecular imaging techniques like NMR, X\u2010ray diffraction and single particle electron microscopy. In cell biology, one goal, often referred to as visual proteomics, is the molecular mapping of whole cells. To achieve this goal and link cryo electron tomography to these high\u2010resolution techniques, increasing the attainable resolution to 2\u20135 nm is vital. Here, we provide an overview of technical factors that limit the resolution in cryo electron tomography and discuss how during data acquisition and image processing these can be optimized to attain the highest possible resolution. Also, existing resolution measurement approaches and current technological developments that potentially increase the resolution in cryo electron tomography are discussed.</jats:p>",
  "DOI": "10.1111/j.1365-2818.2012.03627.x",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2012,
        6,
        7
      ]
    ],
    "date-time": "2012-06-07T10:49:40Z",
    "timestamp": 1339066180000
  },
  "page": "1-5",
  "update-policy": "http://dx.doi.org/10.1002/crossmark_policy",
  "source": "Crossref",
  "is-referenced-by-count": 49,
  "title": "Pushing the resolution limits in cryo electron tomography of biological structures",
  "prefix": "10.1111",
  "volume": "248",
  "author": [
    {
      "given": "CHRISTOPH. A.",
      "family": "DIEBOLDER",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "ABRAHAM J.",
      "family": "KOSTER",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "ROMAN I.",
      "family": "KONING",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2012,
        6,
        7
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_6_2_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.jsb.2005.04.006"
    },
    {
      "key": "e_1_2_6_3_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1098/rspa.1970.0119"
    },
    {
      "key": "e_1_2_6_4_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.jsb.2010.03.013"
    },
    {
      "key": "e_1_2_6_5_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1099/mic.0.28159-0"
    },
    {
      "key": "e_1_2_6_6_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.ultramic.2006.02.004"
    },
    {
      "key": "e_1_2_6_7_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0006-3495(98)74028-7"
    },
    {
      "key": "e_1_2_6_8_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.aanat.2009.04.003"
    },
    {
      "key": "e_1_2_6_9_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jsbi.1997.3933"
    },
    {
      "key": "e_1_2_6_10_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.1076184"
    },
    {
      "key": "e_1_2_6_11_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/nrm1861"
    },
    {
      "key": "e_1_2_6_12_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S1047-8477(02)00033-3"
    },
    {
      "key": "e_1_2_6_13_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0304-3991(84)90057-3"
    },
    {
      "key": "e_1_2_6_14_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.jsb.2009.03.019"
    },
    {
      "key": "e_1_2_6_15_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/j.jsb.2004.10.011"
    },
    {
      "key": "e_1_2_6_16_1",
      "doi-asserted-by": "publisher",
      "DOI": "10.1371/journal.pone.0030249"
    }
  ],
  "container-title": "Journal of Microscopy",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2818.2012.03627.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-2818.2012.03627.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        10,
        14
      ]
    ],
    "date-time": "2023-10-14T22:35:11Z",
    "timestamp": 1697322911000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2818.2012.03627.x"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2012,
        6,
        7
      ]
    ]
  },
  "references-count": 15,
  "journal-issue": {
    "issue": "1",
    "published-print": {
      "date-parts": [
        [
          2012,
          10
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1111/j.1365-2818.2012.03627.x"
  ],
  "URL": "http://dx.doi.org/10.1111/j.1365-2818.2012.03627.x",
  "relation": {},
  "ISSN": [
    "0022-2720",
    "1365-2818"
  ],
  "subject": [],
  "container-title-short": "Journal of Microscopy",
  "published": {
    "date-parts": [
      [
        2012,
        6,
        7
      ]
    ]
  },
  "assertion": [
    {
      "value": "2012-06-07",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}