Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

João M. Dias; Carlos A. Cunha; Susana Teixeira; Gabriela Almeida; Cristina Costa; Jorge Lampreia; José J.G. Moura; Isabel Moura; Maria João Romão

doi:10.1107/S0907444999016066

Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

João M. Dias, Carlos A. Cunha, Susana Teixeira, Gabriela Almeida, Cristina Costa, Jorge Lampreia, José J.G. Moura, Isabel Moura, Maria João Romão

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

6 Citations (Scopus)

Abstract

Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl₂ as precipitants in the presence of 3-(decylmethylammonium)propane-1-sulfonate and belong to the space group P2₁2₁2₁, with unit-cell parameters a = 78.94, b = 104.59, c = 143.18 Å. A complete data set to 2.30 Å resolution was collected using synchrotron radiation at the ESRF. However, the crystals may diffract to beyond 1.7 Å and high-resolution data will be collected in the near future.

Original language	English
Pages (from-to)	215-217
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	56
Issue number	2
DOIs	https://doi.org/10.1107/S0907444999016066
Publication status	Published - Feb 2000
Externally published	Yes

Access to Document

10.1107/S0907444999016066

Cite this

Dias, J. M., Cunha, C. A., Teixeira, S., Almeida, G., Costa, C., Lampreia, J., Moura, J. J. G., Moura, I., & Romão, M. J. (2000). Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774. Acta Crystallographica Section D: Biological Crystallography, 56(2), 215-217. https://doi.org/10.1107/S0907444999016066

@article{eee16d34a49e4523a5d3b8e51ec05fe3,

title = "Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774",

abstract = "Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl2 as precipitants in the presence of 3-(decylmethylammonium)propane-1-sulfonate and belong to the space group P212121, with unit-cell parameters a = 78.94, b = 104.59, c = 143.18 {\AA}. A complete data set to 2.30 {\AA} resolution was collected using synchrotron radiation at the ESRF. However, the crystals may diffract to beyond 1.7 {\AA} and high-resolution data will be collected in the near future.",

author = "Dias, {Jo{\~a}o M.} and Cunha, {Carlos A.} and Susana Teixeira and Gabriela Almeida and Cristina Costa and Jorge Lampreia and Moura, {Jos{\'e} J.G.} and Isabel Moura and Rom{\~a}o, {Maria Jo{\~a}o}",

year = "2000",

month = feb,

doi = "10.1107/S0907444999016066",

language = "English",

volume = "56",

pages = "215--217",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "John Wiley & Sons Inc.",

number = "2",

}

Dias, JM, Cunha, CA, Teixeira, S, Almeida, G, Costa, C, Lampreia, J, Moura, JJG, Moura, I & Romão, MJ 2000, 'Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774', Acta Crystallographica Section D: Biological Crystallography, vol. 56, no. 2, pp. 215-217. https://doi.org/10.1107/S0907444999016066

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

AU - Dias, João M.

AU - Cunha, Carlos A.

AU - Teixeira, Susana

AU - Almeida, Gabriela

AU - Costa, Cristina

AU - Lampreia, Jorge

AU - Moura, José J.G.

AU - Moura, Isabel

AU - Romão, Maria João

PY - 2000/2

Y1 - 2000/2

N2 - Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl2 as precipitants in the presence of 3-(decylmethylammonium)propane-1-sulfonate and belong to the space group P212121, with unit-cell parameters a = 78.94, b = 104.59, c = 143.18 Å. A complete data set to 2.30 Å resolution was collected using synchrotron radiation at the ESRF. However, the crystals may diffract to beyond 1.7 Å and high-resolution data will be collected in the near future.

AB - Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl2 as precipitants in the presence of 3-(decylmethylammonium)propane-1-sulfonate and belong to the space group P212121, with unit-cell parameters a = 78.94, b = 104.59, c = 143.18 Å. A complete data set to 2.30 Å resolution was collected using synchrotron radiation at the ESRF. However, the crystals may diffract to beyond 1.7 Å and high-resolution data will be collected in the near future.

UR - http://www.scopus.com/inward/record.url?scp=0034141953&partnerID=8YFLogxK

U2 - 10.1107/S0907444999016066

DO - 10.1107/S0907444999016066

M3 - Article

C2 - 10666610

AN - SCOPUS:0034141953

SN - 0907-4449

VL - 56

SP - 215

EP - 217

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 2

ER -

Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774

Abstract

Access to Document

Other files and links

Fingerprint

Cite this