title: Preliminary crystallographic study of pyrimidine dimer-specific excision-repair enzyme from bacteriophage T4.
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.
authors.affiliation: Protein Engineering Research Institute, Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Morikawa
authors.forename: M
authors.initials: M
authors.lastname: Tsujimoto
authors.forename: M
authors.initials: M
authors.lastname: Ikehara
authors.forename: T
authors.initials: T
authors.lastname: Inaoka
authors.forename: E
authors.initials: E
authors.lastname: Ohtsuka
mesh_terms: D003461:Crystallography; D004260:DNA Repair; D004279:DNA, Viral / Q000378:metabolism; D043224:Deoxyribonuclease (Pyrimidine Dimer); D004706:Endodeoxyribonucleases; D011740:Pyrimidine Dimers / Q000378:metabolism*; D013604:T-Phages / Q000201:enzymology*; D014764:Viral Proteins
chemical_list: D004279:DNA, Viral; D011740:Pyrimidine Dimers; D014764:Viral Proteins; D004706:Endodeoxyribonucleases; C470698:endonuclease V, phage T4; D043224:Deoxyribonuclease (Pyrimidine Dimer)