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SAD phasing towards structure determination of a thermostable Rieske ferredoxin with a novel stabilizing disulfide bridge
Author(s) -
Bandeiras Tiago M.,
Freitas Micael C.,
Petrasch Dennis,
Kletzin Arnulf,
Frazão Carlos
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113008385
Subject(s) - ferredoxin , electron transfer , crystallography , disulfide bond , chemistry , cysteine , biochemistry , photochemistry , enzyme
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 C x 3 C 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  K α edge led to solution of the phase problem.

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