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Crystallization and preliminary X-ray characterization of a ferritin from the hyperthermophilic archaeon and anaerobe Pyrococcus furiosus.

Identifieur interne : 002F17 ( Main/Exploration ); précédent : 002F16; suivant : 002F18

Crystallization and preliminary X-ray characterization of a ferritin from the hyperthermophilic archaeon and anaerobe Pyrococcus furiosus.

Auteurs : Pedro M. Matias [Portugal] ; Jana Tatur ; Maria Arménia Carrondo ; Wilfred R. Hagen

Source :

RBID : pubmed:16511080

Descripteurs français

English descriptors

Abstract

Crystals of the title protein have been produced and preliminary structural analysis has been carried out. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 258.1, b = 340.1, c = 266.5 A. The protein forms a 24-mer of 20 kDa subunits, which assemble with 432 non-crystallographic symmetry. A total of 36 monomers are found in the asymmetric unit, corresponding to one and a half 24-mers.

DOI: 10.1107/S1744309105011516
PubMed: 16511080


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<nlm:affiliation>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. República, EAN, 2784-505 Oeiras, Portugal. matias@itqb.unl.pt</nlm:affiliation>
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<term>Crystallography, X-Ray</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Ferritins (chemistry)</term>
<term>Ferritins (genetics)</term>
<term>Ferritins (isolation & purification)</term>
<term>Ferritins (metabolism)</term>
<term>Iron (metabolism)</term>
<term>Protein Conformation</term>
<term>Protein Subunits (chemistry)</term>
<term>Pyrococcus furiosus (enzymology)</term>
<term>Pyrococcus furiosus (metabolism)</term>
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<term>Archéobactéries (enzymologie)</term>
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<term>Escherichia coli (génétique)</term>
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<term>Ferritines</term>
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<term>Escherichia coli</term>
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<div type="abstract" xml:lang="en">Crystals of the title protein have been produced and preliminary structural analysis has been carried out. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 258.1, b = 340.1, c = 266.5 A. The protein forms a 24-mer of 20 kDa subunits, which assemble with 432 non-crystallographic symmetry. A total of 36 monomers are found in the asymmetric unit, corresponding to one and a half 24-mers.</div>
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