Literature DB >> 3172233

Preliminary crystallographic study of pyrimidine dimer-specific excision-repair enzyme from bacteriophage T4.

K Morikawa1, M Tsujimoto, M Ikehara, T Inaoka, E Ohtsuka.   

Abstract

Bacteriophage T4 endonuclease V, which is an excision-repair enzyme specific to pyrimidine dimers within DNA, has been crystallized from polyethylene glycol 4000 solution by a vapour diffusion technique. The unit cell is monoclinic, space group P2(1), with unit cell parameters: a = 41.4 A, b = 40.1 A, c = 37.5 A, beta = 90.01 degrees. The unit cell contains two 16,000 Mr molecules. The crystals diffract X-rays beyond 2.3 A resolution and are suitable for structural analysis at high resolution.

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Year:  1988        PMID: 3172233     DOI: 10.1016/0022-2836(88)90298-7

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  1 in total

1.  Role of the basic amino acid cluster and Glu-23 in pyrimidine dimer glycosylase activity of T4 endonuclease V.

Authors:  T Doi; A Recktenwald; Y Karaki; M Kikuchi; K Morikawa; M Ikehara; T Inaoka; N Hori; E Ohtsuka
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-15       Impact factor: 11.205

  1 in total

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