DOI: 10.1073/pnas.81.14.4378. Crystallization of myosin subfragment 1.

Crystallization of myosin subfragment 1.

10.1073/pnas.81.14.4378

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Crystals of myosin subfragment 1 from avian skeletal muscle have been grown reproducibly. They diffract x-rays to at least 4.5-A resolution. The subfragment 1 crystallizes in space group P2(1)2(1)2(1) where a = 107 A, b = 117 A, and c = 278 A. The cell dimensions and intensity distribution on x-ray diffraction photographs are consistent with two molecules in the crystallographic asymmetric unit. Electrophoretic analysis shows that the myosin subfragment 1 present in the crystals contains a 95-kilodalton heavy chain fragment and both the essential and regulatory light chains.

Bibliography

Rayment, I., & Winkelmann, D. A. (1984). Crystallization of myosin subfragment 1. Proceedings of the National Academy of Sciences, 81(14), 4378â4380.

Authors 2

I Rayment (first)
D A Winkelmann (additional)

References 0 Referenced 27

None

Dates

Type	When
Created	19 years, 2 months ago (May 31, 2006, 5:27 a.m.)
Deposited	3 years, 4 months ago (April 13, 2022, 12:03 p.m.)
Indexed	1 year, 1 month ago (July 10, 2024, 4:38 p.m.)
Issued	41 years, 1 month ago (July 1, 1984)
Published	41 years, 1 month ago (July 1, 1984)
Published Online	41 years, 1 month ago (July 1, 1984)
Published Print	41 years, 1 month ago (July 1, 1984)

Funders 0

None

BibTeX

@article{Rayment_1984, title={Crystallization of myosin subfragment 1.}, volume={81}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.81.14.4378}, DOI={10.1073/pnas.81.14.4378}, number={14}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Rayment, I and Winkelmann, D A}, year={1984}, month=jul, pages={4378–4380} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2024,
        7,
        10
      ]
    ],
    "date-time": "2024-07-10T20:38:00Z",
    "timestamp": 1720643880680
  },
  "reference-count": 0,
  "publisher": "Proceedings of the National Academy of Sciences",
  "issue": "14",
  "content-domain": {
    "domain": [
      "www.pnas.org"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1984,
        7
      ]
    ]
  },
  "abstract": "<jats:p>Crystals of myosin subfragment 1 from avian skeletal muscle have been grown reproducibly. They diffract x-rays to at least 4.5-A resolution. The subfragment 1 crystallizes in space group P2(1)2(1)2(1) where a = 107 A, b = 117 A, and c = 278 A. The cell dimensions and intensity distribution on x-ray diffraction photographs are consistent with two molecules in the crystallographic asymmetric unit. Electrophoretic analysis shows that the myosin subfragment 1 present in the crystals contains a 95-kilodalton heavy chain fragment and both the essential and regulatory light chains.</jats:p>",
  "DOI": "10.1073/pnas.81.14.4378",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2006,
        5,
        31
      ]
    ],
    "date-time": "2006-05-31T09:27:08Z",
    "timestamp": 1149067628000
  },
  "page": "4378-4380",
  "update-policy": "http://dx.doi.org/10.1073/pnas.cm10313",
  "source": "Crossref",
  "is-referenced-by-count": 27,
  "title": "Crystallization of myosin subfragment 1.",
  "prefix": "10.1073",
  "volume": "81",
  "author": [
    {
      "given": "I",
      "family": "Rayment",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "D A",
      "family": "Winkelmann",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "341",
  "published-online": {
    "date-parts": [
      [
        1984,
        7
      ]
    ]
  },
  "container-title": "Proceedings of the National Academy of Sciences",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://pnas.org/doi/pdf/10.1073/pnas.81.14.4378",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2022,
        4,
        13
      ]
    ],
    "date-time": "2022-04-13T16:03:10Z",
    "timestamp": 1649865790000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://pnas.org/doi/full/10.1073/pnas.81.14.4378"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1984,
        7
      ]
    ]
  },
  "references-count": 0,
  "journal-issue": {
    "issue": "14",
    "published-print": {
      "date-parts": [
        [
          1984,
          7
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1073/pnas.81.14.4378"
  ],
  "URL": "http://dx.doi.org/10.1073/pnas.81.14.4378",
  "relation": {},
  "ISSN": [
    "0027-8424",
    "1091-6490"
  ],
  "subject": [],
  "container-title-short": "Proc. Natl. Acad. Sci. U.S.A.",
  "published": {
    "date-parts": [
      [
        1984,
        7
      ]
    ]
  },
  "assertion": [
    {
      "value": "1984-07-01",
      "order": 2,
      "name": "published",
      "label": "Published",
      "group": {
        "name": "publication_history",
        "label": "Publication History"
      }
    }
  ]
}