Crystallization and preliminary X-ray diffraction analysis of the small subunit of the heterodimeric restriction endonuclease R.BspD6I.
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.
Kachalova
Galina S
GS
Max-Planck Unit for Structural Molecular Biology, Hamburg 22607, Germany.
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
D003460:Crystallization; D004262:DNA Restriction Enzymes / Q000737:chemistry / Q000302:isolation & purification; D003850:Deoxyribonuclease I / Q000737:chemistry* / Q000302:isolation & purification; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D021122:Protein Subunits / Q000737:chemistry; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; D021122:Protein Subunits; D004262:DNA Restriction Enzymes; D003850:Deoxyribonuclease I; C514554:BspD6I protein, E coli