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 | |
| Publication status | Published - 1997 |
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Keywords
- crystal growth
- dimeric bacterial hemoglobin
- Vitreoscilla stercoraria
- x- ray diffraction
ASJC Scopus subject areas
- Genetics
- Structural Biology
- Biochemistry
Cite this
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
}
TY - JOUR
T1 - Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria
AU - Tarricone, Cataldo
AU - Calogero, Sabina
AU - Galizzi, Alessandro
AU - Coda, Alessandro
AU - Ascenzi, Paolo
AU - Bolognesi, Martino
PY - 1997
Y1 - 1997
N2 - 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%.
AB - 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%.
KW - crystal growth
KW - dimeric bacterial hemoglobin
KW - Vitreoscilla stercoraria
KW - x- ray diffraction
UR - http://www.scopus.com/inward/record.url?scp=0031022957&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031022957&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M
DO - 10.1002/(SICI)1097-0134(199701)27:1<154::AID-PROT15>3.0.CO;2-M
M3 - Article
VL - 27
SP - 154
EP - 156
JO - Proteins: Structure, Function and Genetics
JF - Proteins: Structure, Function and Genetics
SN - 0887-3585
IS - 1
ER -