Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1493-5. Epub 2003 Jul 23.

Crystallization of restriction endonuclease SfiI in complex with DNA.

Viadiu H, Vanamee ES, Jacobson EM, Schildkraut I, Aggarwal AK.

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Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029, USA.

Abstract

The SfiI endonuclease from Streptomyces fimbriatus (EC 3.1.21.4) is a tetrameric enzyme that binds simultaneously to two recognition sites and cleaves both sites concertedly. It serves as a good model system for studying both specificity and cooperative DNA binding. Crystals of the enzyme were obtained by the hanging-drop vapor-diffusion method in complex with a 21-mer oligonucleotide. The crystals are trigonal, with unit-cell parameters a = b = 85.7, c = 202.6 A, and diffract to 2.6 A resolution on a rotating-anode X-ray generator. Preliminary X-ray analysis reveals the space group to be either P3(1)21 or P3(2)21. Interestingly, the crystals change to space group P6(1)22, with unit-cell parameters a = b = 85.5, c = 419.6 A, when the selenomethionyl (SeMet) derivative of the enzyme is co-crystallized with the same DNA. Phase information is currently being derived from this SeMet SfiI-DNA complex.

PMID:: 12876363; [PubMed - indexed for MEDLINE]

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Cited by 1 PubMed Central article

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