Crystallization and preliminary X-ray studies of recombinant human granulocyte-macrophage colony stimulating factor

Judith M. La Londe; Lewis S. Hanna; Rosemarie Rattoballi; Helen M. Berman; Donald Voet

doi:10.1016/0022-2836(89)90323-9

Crystallization and preliminary X-ray studies of recombinant human granulocyte-macrophage colony stimulating factor

Judith M. La Londe, Lewis S. Hanna, Rosemarie Rattoballi, Helen M. Berman, Donald Voet

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

6 Scopus citations

Abstract

Human granulocyte-macrophage colony stimulating factor (hGM-CSF) is an important regulator of growth and differentiation for mononuclear and polymorphonuclear phagocytes. Here we report the crystallization and preliminary X-ray studies of Escherichia coli-expressed hGM-CSF. The crystals are orthorhombic, with the space group P2₁2₁2₁, and have unit cell dimensions a = 46.62 A ̊, b = 58.73 A ̊ and c = 126.42 A ̊. Recombinant hGM-CSF crystals diffract X-rays to 2.4 Å resolution and are thus suitable for X-ray structural studies.

Original language	English (US)
Pages (from-to)	783-785
Number of pages	3
Journal	Journal of molecular biology
Volume	205
Issue number	4
DOIs	https://doi.org/10.1016/0022-2836(89)90323-9
State	Published - Feb 20 1989
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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title = "Crystallization and preliminary X-ray studies of recombinant human granulocyte-macrophage colony stimulating factor",

abstract = "Human granulocyte-macrophage colony stimulating factor (hGM-CSF) is an important regulator of growth and differentiation for mononuclear and polymorphonuclear phagocytes. Here we report the crystallization and preliminary X-ray studies of Escherichia coli-expressed hGM-CSF. The crystals are orthorhombic, with the space group P212121, and have unit cell dimensions a = 46.62 A ̊, b = 58.73 A ̊ and c = 126.42 A ̊. Recombinant hGM-CSF crystals diffract X-rays to 2.4 {\AA} resolution and are thus suitable for X-ray structural studies.",

author = "{La Londe}, {Judith M.} and Hanna, {Lewis S.} and Rosemarie Rattoballi and Berman, {Helen M.} and Donald Voet",

note = "Funding Information: We thank Dr Vincent L. Giranda for helpful discussions. The research reported here was partly supported by grants to H.M.B. from NIH GM21589, CA06927, RR05539, and by an appropriation of the Commonwealth of Pennsylvania.",

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doi = "10.1016/0022-2836(89)90323-9",

language = "English (US)",

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pages = "783--785",

journal = "Journal of Molecular Biology",

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T1 - Crystallization and preliminary X-ray studies of recombinant human granulocyte-macrophage colony stimulating factor

AU - La Londe, Judith M.

AU - Hanna, Lewis S.

AU - Rattoballi, Rosemarie

AU - Berman, Helen M.

AU - Voet, Donald

N1 - Funding Information: We thank Dr Vincent L. Giranda for helpful discussions. The research reported here was partly supported by grants to H.M.B. from NIH GM21589, CA06927, RR05539, and by an appropriation of the Commonwealth of Pennsylvania.

PY - 1989/2/20

Y1 - 1989/2/20

N2 - Human granulocyte-macrophage colony stimulating factor (hGM-CSF) is an important regulator of growth and differentiation for mononuclear and polymorphonuclear phagocytes. Here we report the crystallization and preliminary X-ray studies of Escherichia coli-expressed hGM-CSF. The crystals are orthorhombic, with the space group P212121, and have unit cell dimensions a = 46.62 A ̊, b = 58.73 A ̊ and c = 126.42 A ̊. Recombinant hGM-CSF crystals diffract X-rays to 2.4 Å resolution and are thus suitable for X-ray structural studies.

AB - Human granulocyte-macrophage colony stimulating factor (hGM-CSF) is an important regulator of growth and differentiation for mononuclear and polymorphonuclear phagocytes. Here we report the crystallization and preliminary X-ray studies of Escherichia coli-expressed hGM-CSF. The crystals are orthorhombic, with the space group P212121, and have unit cell dimensions a = 46.62 A ̊, b = 58.73 A ̊ and c = 126.42 A ̊. Recombinant hGM-CSF crystals diffract X-rays to 2.4 Å resolution and are thus suitable for X-ray structural studies.

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Crystallization and preliminary X-ray studies of recombinant human granulocyte-macrophage colony stimulating factor

Abstract

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