Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria

Cataldo Tarricone; Sabina Calogero; Alessandro Galizzi; Alessandro Coda; Paolo Ascenzi; Martino Bolognesi

doi:10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M

Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria

Cataldo Tarricone, Sabina Calogero, Alessandro Galizzi, Alessandro Coda, Paolo Ascenzi, Martino Bolognesi

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

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

Abstract

The recombinant homodimeric hemoglobin from the strictly aerobe gram- negative bacterium Vitreoscilla stercoraria has been expressed in Escherichia coli, purified to homogeneity, and crystallized by vapor diffusion techniques, using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2₁ and diffract to HIGH resolution. The unit cell parameters are a = 62.9, b = 42.5, c = 63.2 Å, β = 106.6°; the asymmetric unit contains the homodimeric hemoglobin, with a volume solvent content of 42%.

Original language	English
Pages (from-to)	154-156
Number of pages	3
Journal	Proteins: Structure, Function and Genetics
Volume	27
Issue number	1
DOIs	https://doi.org/10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M
Publication status	Published - 1997

Keywords

crystal growth
dimeric bacterial hemoglobin
Vitreoscilla stercoraria
x- ray diffraction

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M

Cite this

Tarricone, C., Calogero, S., Galizzi, A., Coda, A., Ascenzi, P., & Bolognesi, M. (1997). Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria. Proteins: Structure, Function and Genetics, 27(1), 154-156. https://doi.org/10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M

Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria. / Tarricone, Cataldo; Calogero, Sabina; Galizzi, Alessandro; Coda, Alessandro; Ascenzi, Paolo; Bolognesi, Martino.

In: Proteins: Structure, Function and Genetics, Vol. 27, No. 1, 1997, p. 154-156.

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

Tarricone, C, Calogero, S, Galizzi, A, Coda, A, Ascenzi, P & Bolognesi, M 1997, 'Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria', Proteins: Structure, Function and Genetics, vol. 27, no. 1, pp. 154-156. https://doi.org/10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M

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abstract = "The recombinant homodimeric hemoglobin from the strictly aerobe gram- negative bacterium Vitreoscilla stercoraria has been expressed in Escherichia coli, purified to homogeneity, and crystallized by vapor diffusion techniques, using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P21 and diffract to HIGH resolution. The unit cell parameters are a = 62.9, b = 42.5, c = 63.2 {\AA}, β = 106.6°; the asymmetric unit contains the homodimeric hemoglobin, with a volume solvent content of 42%.",

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AU - Coda, Alessandro

AU - Ascenzi, Paolo

AU - Bolognesi, Martino

PY - 1997

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KW - x- ray diffraction

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Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria

Abstract

Keywords

ASJC Scopus subject areas

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