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SAD phasing towards structure determination of a thermostable Rieske ferredoxin with a novel stabilizing disulfide bridge.

Bandeiras, Tiago M. and Freitas, Micael C. and Petrasch, Dennis and Kletzin, Arnulf and Frazão, Carlos (2013):
SAD phasing towards structure determination of a thermostable Rieske ferredoxin with a novel stabilizing disulfide bridge.
69, In: Acta crystallographica. Section F, Structural biology and crystallization communications, (Pt 5), pp. 555-8, ISSN 1744-3091, [Article]

Abstract

Rieske proteins and Rieske ferredoxins are ubiquitous electron-transfer metalloproteins that are characterized by a [2Fe-2S] cluster coordinated by pairs of cysteine and histidine residues. The thermoacidophilic archaeon Acidianus ambivalens contains a Rieske ferredoxin termed RFd2, which has an hitherto unknown additional region of 40-44 residues at the C-terminus with a Cx3C motif that introduces a novel disulfide bond within the Rieske fold. RFd2 was crystallized with the aim of determining its three-dimensional structure in order to understand the contribution of this as yet unique disulfide bridge to the function and stability of RFd2. RFd2 crystals were successively improved, increasing their diffraction to 1.9 Å resolution. Molecular replacement did not solve the RFd2 structure, but a highly multiple in-house diffraction data set collected at the Cu Kα edge led to solution of the phase problem.

Item Type: Article
Erschienen: 2013
Creators: Bandeiras, Tiago M. and Freitas, Micael C. and Petrasch, Dennis and Kletzin, Arnulf and Frazão, Carlos
Title: SAD phasing towards structure determination of a thermostable Rieske ferredoxin with a novel stabilizing disulfide bridge.
Language: English
Abstract:

Rieske proteins and Rieske ferredoxins are ubiquitous electron-transfer metalloproteins that are characterized by a [2Fe-2S] cluster coordinated by pairs of cysteine and histidine residues. The thermoacidophilic archaeon Acidianus ambivalens contains a Rieske ferredoxin termed RFd2, which has an hitherto unknown additional region of 40-44 residues at the C-terminus with a Cx3C motif that introduces a novel disulfide bond within the Rieske fold. RFd2 was crystallized with the aim of determining its three-dimensional structure in order to understand the contribution of this as yet unique disulfide bridge to the function and stability of RFd2. RFd2 crystals were successively improved, increasing their diffraction to 1.9 Å resolution. Molecular replacement did not solve the RFd2 structure, but a highly multiple in-house diffraction data set collected at the Cu Kα edge led to solution of the phase problem.

Journal or Publication Title: Acta crystallographica. Section F, Structural biology and crystallization communications
Volume: 69
Number: Pt 5
Divisions: 10 Department of Biology
10 Department of Biology > Sulfur Biochemistry and Microbial Bioenergetics
Date Deposited: 02 Jul 2013 12:47
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