PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA-FASCICULATA

被引:15
作者
KURIYAN, J [1 ]
WONG, L [1 ]
GUENTHER, BD [1 ]
MURGOLO, NJ [1 ]
CERAMI, A [1 ]
HENDERSON, GB [1 ]
机构
[1] ROCKEFELLER UNIV,MED BIOCHEM LAB,NEW YORK,NY 10021
关键词
D O I
10.1016/S0022-2836(05)80353-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Trypanothione reductase, a flavoprotein disulfide reductase specific to trypanosomatid parasites, has been crystallized by vapor diffusion of a protein solution (10 mg/ml) against 22% polyethylene glycol (average Mr 8000) containing 100 mm-ammonium sulfate. Crystals of a size suitable for structure determination by X-ray diffraction have been obtained by seeding protein solutions with smaller crystals. The space-group is P21 (a=60·9 , b=161·8 , c=58·4 , β=99·10). The molecular mass and volume of the unit cell suggest that there is a dimer of the enzyme in the asymmetric unit, and this is confirmed by self-rotation functions calculated using data to 4·5resolution. The crystals diffract to beyond 3resolution. Crystals of another P21 form (a=91·3 , b=114·4 , c=92·0β=141·30) are observed to grow under similar conditions. © 1990, Academic Press Limited. All rights reserved.
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页码:335 / 337
页数:3
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