| Autor: |
O'Loughlin TJ; Department of Physiology and Structural Biology, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118-2526, USA., Xu Q, Kucera RB, Dorner LF, Sweeney S, Schildkraut I, Guo HC |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2000 Dec; Vol. 56 (Pt 12), pp. 1652-5. |
| DOI: |
10.1107/s0907444900012713 |
| Abstrakt: |
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%. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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