Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/96386
Type: Artigo de periódico
Title: Crystallization And X-ray Crystallographic Analysis Of Recombinant Chicken Poly (adp-ribose) Polymerase Catalytic Domain Produced In Sf9 Insect Cells
Author: Jung S.
Miranda E.A.
De Murcia J.M.
Niedergang C.
Delarue M.
Schulz G.E.
De Murcia G.M.
Abstract: Poly (ADP-ribose) polymerase (PARP) participates in the immediate response in mammalian cells exposed to DNA-damaging agents. Recombinant baculovirus harboring the cDNA of the chicken PARP catalytic domain (40 kDa) have been used to infect Spodoptera frugiperda (Sf9) insect cells. The recombinant polypeptide (30 mg per 1x109 cells) was purified to homogeneity by 3-aminobenzamide affinity chromatography. The enzymatic properties of the recombinant domain were similar to those of the native fragment. Crystals of the purified recombinant catalytic domain were grown by vapor diffusion. The crystals belong to space group P212121 with unit cell dimensions of a = 59.2 Å, b = 65.0 Å, c = 96.9 Å. They aresuitable for X-ray analysis and diffract to 2.0 Å.
Editor: 
Rights: fechado
Identifier DOI: 10.1006/jmbi.1994.1709
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0027948288&partnerID=40&md5=77995f78c510c861fb2d3666672d29dd
Date Issue: 1994
Appears in Collections:Unicamp - Artigos e Outros Documentos

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