CRYSTALLIZATION OF INHIBITED ASPARTIC PROTEINASE FROM CANDIDA-ALBICANS

被引：14

作者：

CUTFIELD, S ^{[1
]}

MARSHALL, C ^{[1
]}

MOODY, P ^{[1
]}

SULLIVAN, P ^{[1
]}

CUTFIELD, J ^{[1
]}

机构：

[1] UNIV YORK,DEPT CHEM,YORK YO1 5DD,N YORKSHIRE,ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 234卷 / 04期

关键词：

ASPARTIC PROTEINASE; CANDIDA-ALBICANS; PEPSTATIN; A70450; CRYSTALLIZATION;

D O I：

10.1006/jmbi.1993.1679

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：

A major secreted aspartic proteinase from Candida albicans has been crystallized in the presence of inhibitors to prevent autodegradation. With pepstatin a cleaved form of the enzyme was nevertheless found in the crystals whereas with the inhibitor A70450 the enzyme remained intact. The crystals containing pepstatin were not suitable for X-ray data collection while thecrystals containing A70450 grew by vapour diffusion as tetragonal bipyramids, space group P43212 (or P41212), a = b = 76.2 Å, c = 126.1 Å, with one molecule in the asymmetric unit and they diffract to beyond 2.2 Å. © 1993 Academic Press Limited.

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页码：1266 / 1269

页数：4

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