CRYSTALLIZATION OF AN ENDOCHITINASE FROM HORDEUM-VULGARE L SEEDS

被引：7

作者：

HART, PJ ^{[1
]}

READY, MP ^{[1
]}

ROBERTUS, JD ^{[1
]}

机构：

[1] UNIV TEXAS,CLAYTON FDN BIOCHEM INST,DEPT CHEM & BIOCHEM,AUSTIN,TX 78712

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 225卷 / 02期

关键词：

CRYSTALLIZATION; X-RAY ANALYSIS; ENDOCHITINASE; BARLEY;

D O I：

10.1016/0022-2836(92)90942-D

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：

Higher plants contain several constitutively expressed proteins for protection against infections by viruses, bacteria and fungi. Here we report the crystallization of a polypeptide with antifungal activity, a 26,000 dalton endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for high-resolution X-ray analysis. Crystals were grown by vapor diffusion under several different conditions. The best crystals, obtained with ammonium sulfate as the precipitant, belong to the tetragonal space group P412121 (P43212). with cell dimensions a = b = 62.9 A ̊and c = 96.0 A ̊. The cell dimensions are consistent with one endochitinase molecule per asymmetric unit, and the crystals diffract to at least 2.0 Å resolution. © 1992.

引用

页码：565 / 567

页数：3

共 15 条

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