Crystallization and preliminary X-ray diffraction analysis of MspI restriction endonuclease in complex with its cognate DNA.
Acta Crystallogr D Biol Crystallogr
; 56(Pt 12): 1652-5, 2000 Dec.
Article
em En
| MEDLINE
| ID: mdl-11092936
ABSTRACT
The MspI restriction endonuclease is a type II restriction enzyme. Unlike all other restriction enzymes with known structures, MspI recognizes the palindromic tetranucleotide sequence 5'-C/CGG and cleaves it as indicated by the '/' to produce DNA products with 5' two-base overhangs. Owing to the nature of its cleavage pattern, it is likely that MspI would represent a new structural class of restriction endonucleases. Crystals of the dimeric MspI restriction enzyme bound to a duplex DNA molecule containing the specific recognition sequence have been obtained by vapor-diffusion techniques in the presence of polyethylene glycol as precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 50.2, b = 131.6, c = 59.3 A, beta = 109.7 degrees. The crystals contain one dimeric complex in the asymmetric unit. A complete native data set has been collected to a resolution of 2.05 A by cryo-crystallographic methods, with an R(merge) of 4.0%.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
DNA
/
Desoxirribonuclease HpaII
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2000
Tipo de documento:
Article