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TRYPANOSOMA-CRUZI TRYPANOTHIONE REDUCTASE - CRYSTALLIZATION, UNIT-CELL DIMENSIONS AND STRUCTURE SOLUTION

被引：8
作者：
ZHANG, YH
BAILEY, S
NAISMITH, JH
BOND, CS
HABASH, J
MCLAUGHLIN, P
PAPIZ, MZ
BORGES, A
CUNNINGHAM, M
FAIRLAMB, AH
HUNTER, WN
机构：
[1] UNIV MANCHESTER,DEPT CHEM,OXFORD RD,MANCHESTER M13 9PL,LANCS,ENGLAND
[2] ADDENBROOKES HOSP,MRC,MOLEC BIOL LAB,CAMBRIDGE CB1 3QH,ENGLAND
[3] SERC,DARESBURY LAB,WARRINGTON WA4 4AD,CHESHIRE,ENGLAND
[4] UNIV LONDON LONDON SCH HYG & TROP MED,DEPT MED PARASITOL,LONDON WC1E 7HT,ENGLAND
来源：
JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 232卷 / 04期
基金：
英国惠康基金;
关键词：
MOLECULAR REPLACEMENT; PROTEIN CRYSTALLIZATION; TRYPANOTHIONE REDUCTASE; X-RAY DIFFRACTION;
D O I：
10.1006/jmbi.1993.1475
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：
We have reproducibly crystallized recombinant trypanothione reductase from Trypanosoma cruzi. Yellow tetragonal crystals in the shape of elongated prisms have unit cell dimensions of a=92.8 Å, c=156.6 Å. Laue symmetry of 4/m and are suitable for a detailed structural analysis. Diffraction data to 2.7 Å resolution have been recorded using synchrotron radiation at the Daresbury laboratory. The structure has been solved by molecular replacement calculations using this synchrotron data and our previously determined Crithidia fasciculata enzyme structure as a search model. The space group has been identified as P43 with a homodimer of approximate molecular mass of 108 kDa in the asymmetric unit. Diffraction beyond 2.5 Å has been recorded when large freshly grown crystals are exposed to X-rays. Refinement of the structure is in progress. © 1993 Academic Press Limited.
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页码：1217 / 1220
页数：4
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