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Crystallization and preliminary X-ray crystallographic studies of a complex between the Lactococcus lactis Fpg DNA-repair enzyme and an abasic site containing DNA by Karine Pereira de Jésus; Laurence Serre; Nadège Hervouet; Véronique Bouckson-Castaing; Charles Zelwer; Bertrand Castaing is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Crystallization and preliminary X-ray crystallographic studies of a complex between the Lactococcus lactis Fpg DNA-repair enzyme and an abasic site containing DNA about?

For protein±DNA complex crystallization, the choice of the DNA fragment is crucial. With the aim of crystallizing the 31 kDa Fpg DNA-repair enzyme bound to DNA, oligonucleotide duplexes varying in length, sequence, end type and nature of the speci®c DNA target site were used. Crystals of several protein±DNA combinations grew from solutions containing both polyethylene glycol and salt. This systematic crystallization screening followed by optimization of the crystallization conditions by microseeding led to crystals of Fpg bound to a 13 base-pair duplex DNA carrying the 1,3-propanediol abasic site analogue which are suitable for crystallographic analysis. Complete native data sets have been collected to 2.1 A Ê resolution.

Who reads Crystallization and preliminary X-ray crystallographic studies of a complex between the Lactococcus lactis Fpg DNA-repair enzyme and an abasic site containing DNA?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Karine Pereira de Jésus; Laurence Serre; Nadège Hervouet; Véronique Bouckson-Castaing; Charles Zelwer; Bertrand Castaing
Publisher
International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)
Published
2002
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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