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Title 

Purification, crystallization and data collection of the apoptotic nuclease endonuclease G

Authors 

Sei Mee YoonHyung Nam SongJ H YangM Y LimY J ChungSeong Eon RyuEui-jeon Woo

Publisher 

International Union of Crystallography

Issue Date 

2009

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 65, no. 5, pp. 504-507

Abstract 

Endonuclease G (EndoG) is a mitochondrial enzyme that responds to apoptotic stimuli by translocating to the nucleus and cleaving chromosomal DNA. EndoG is the main apoptotic endonuclease in the caspase-independent pathway. Mouse EndoG without the mitochondrial localization signal (amino-acid residues 1-43) was successfully overexpressed, purified and crystallized using a microbatch method under oil. The initial crystal (type I) was grown in the presence of the detergent CTAB and diffracted to 2.8 A resolution, with unit-cell parameters a = 72.20, b = 81.88, c = 88.66 A, beta = 97.59 degrees in a monoclinic space group. The crystal contained two monomers in the asymmetric unit, with a predicted solvent content of 46.6%. Subsequent mutation of Cys110 improved the stability of the protein significantly and produced further crystals of types II, III and IV with space groups C2, P4(1)2(1)2 (or P4(3)2(1)2) and P2(1)2(1)2(1), respectively, in various conditions. This suggests the critical involvement of this conserved cysteine residue in the crystallization process.

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 65(5): 504-507

ISSN 

1744-3091

Link 

http://dx.doi.org/10.1107/S1744309109013335

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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