A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state

Se Won Suh, Duilio Cascio, Michael Chapman, David Eisenberg

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A new crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC4.1.1.39) from Nicotiana tabacum has been obtained at alkaline pH with polyethylene glycol 8000 in the presence of a non-ionic detergent, β-octyl glucoside. The crystals are grown at room temperature by the hanging-drop vapor diffusion technique from a protein solution containing enzyme complexed with CO2, Mg2+, and the transition state analog 2-C-carboxy-d-arabinitol-1,5-bisphosphate. The crystals belong to the the space group P3121 (or P3221) with the cell parameters a = 204.6 A ̊, and c= 117.4 A ̊ (1 A ̊ = 0.1 nm). The asymmetric unit contains half (L4S4: L, large subunit, 53,000 Mr; S, small subunit, 15,000 Mr) of a hexadecameric molecule (L8S8, 540,000 Mr). The crystals diffract to at least 2.6 Å Bragg spacing and are suitable for X-ray structure determination.

Original languageEnglish (US)
Pages (from-to)363-365
Number of pages3
JournalJournal of Molecular Biology
Volume197
Issue number2
DOIs
StatePublished - Sep 20 1987
Externally publishedYes

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Oxygenases
Detergents
Tobacco
X-Rays
Temperature
Enzymes
Proteins
polyethylene glycol 8000
ribulose-1,5 diphosphate
octyl-beta-D-glucoside

ASJC Scopus subject areas

  • Virology

Cite this

A crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum in the activated state. / Suh, Se Won; Cascio, Duilio; Chapman, Michael; Eisenberg, David.

In: Journal of Molecular Biology, Vol. 197, No. 2, 20.09.1987, p. 363-365.

Research output: Contribution to journalArticle

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abstract = "A new crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC4.1.1.39) from Nicotiana tabacum has been obtained at alkaline pH with polyethylene glycol 8000 in the presence of a non-ionic detergent, β-octyl glucoside. The crystals are grown at room temperature by the hanging-drop vapor diffusion technique from a protein solution containing enzyme complexed with CO2, Mg2+, and the transition state analog 2-C-carboxy-d-arabinitol-1,5-bisphosphate. The crystals belong to the the space group P3121 (or P3221) with the cell parameters a = 204.6 A ̊, and c= 117.4 A ̊ (1 A ̊ = 0.1 nm). The asymmetric unit contains half (L4S4: L, large subunit, 53,000 Mr; S, small subunit, 15,000 Mr) of a hexadecameric molecule (L8S8, 540,000 Mr). The crystals diffract to at least 2.6 {\AA} Bragg spacing and are suitable for X-ray structure determination.",
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AB - A new crystal form of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC4.1.1.39) from Nicotiana tabacum has been obtained at alkaline pH with polyethylene glycol 8000 in the presence of a non-ionic detergent, β-octyl glucoside. The crystals are grown at room temperature by the hanging-drop vapor diffusion technique from a protein solution containing enzyme complexed with CO2, Mg2+, and the transition state analog 2-C-carboxy-d-arabinitol-1,5-bisphosphate. The crystals belong to the the space group P3121 (or P3221) with the cell parameters a = 204.6 A ̊, and c= 117.4 A ̊ (1 A ̊ = 0.1 nm). The asymmetric unit contains half (L4S4: L, large subunit, 53,000 Mr; S, small subunit, 15,000 Mr) of a hexadecameric molecule (L8S8, 540,000 Mr). The crystals diffract to at least 2.6 Å Bragg spacing and are suitable for X-ray structure determination.

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