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Crystallization and preliminary X-ray diffraction analysis of the small subunit of the heterodimeric restriction endonuclease R.BspD6I.


ABSTRACT: The heterodimeric restriction endonuclease R.BspD6I is composed of a small subunit with a cleavage site and a large subunit, containing a recognition domain and a cleavage domain, that may function separately as a monomeric nicking endonuclease. Here, the crystallization of the small subunit and diffraction data collection to 1.5 A resolution are reported.

SUBMITTER: Kachalova GS 

PROVIDER: S-EPMC2376331 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the small subunit of the heterodimeric restriction endonuclease R.BspD6I.

Kachalova Galina S GS   Yunusova Alfiya K AK   Artyukh Rimma I RI   Rogulin Eugeny A EA   Perevyazova Tatyana A TA   Zheleznaya Ludmila A LA   Matvienko Nickolay I NI   Bartunik Hans D HD  

Acta crystallographica. Section F, Structural biology and crystallization communications 20070831 Pt 9


The heterodimeric restriction endonuclease R.BspD6I is composed of a small subunit with a cleavage site and a large subunit, containing a recognition domain and a cleavage domain, that may function separately as a monomeric nicking endonuclease. Here, the crystallization of the small subunit and diffraction data collection to 1.5 A resolution are reported. ...[more]

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