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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : J Mol Biol.

Crystallization and X-ray crystallographic analysis of recombinant chicken poly(ADP-ribose) polymerase catalytic domain produced in Sf9 insect cells.

Team: Architecture and Dynamics of Biological Macromolecules
Member: Marc Delarue
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in J Mol Biol. - 18 Nov 1994

Jung S, Miranda EA, de Murcia JM, Niedergang C, Delarue M, Schulz GE, de Murcia GM.

Link to Pubmed [PMID] – 7966315

Link to DOI – 10.1006/jmbi.1994.1709

J Mol Biol. 1994 Nov 18;244(1):114-6.

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 1 x 10(9) 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 P2(1)2(1)2(1) with unit cell dimensions of a = 59.2 A, b = 65.0 A, c = 96.9 A. They are suitable for X-ray analysis and diffract to 2.0 A.