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玉米多胺氧化酶的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L.

作者信息

Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A

机构信息

Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Abbiategrasso 207, 27100 Pavia, Italy.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1429-31. doi: 10.1107/s0907444998005836.

Abstract

Polyamine oxidase catalyses the oxidation of the secondary amino group of spermine, spermidine and their acetyl derivatives. The enzyme plays an important role in the regulation of polyamine intracellular concentration and is a member of the family of flavin-containing amine oxidases. Crystals of maize polyamine oxidase have been grown by the hanging-drop vapour-diffusion technique. The crystals are in hexagonal space group P6122 (or P6522) with cell dimensions a = b = 184.6, c = 280.9 A. A native data set has been collected to 2.7 A resolution at a synchrotron radiation source.

摘要

多胺氧化酶催化精胺、亚精胺及其乙酰衍生物仲氨基的氧化反应。该酶在多胺细胞内浓度的调节中起重要作用,是含黄素胺氧化酶家族的成员之一。通过悬滴气相扩散技术培养出了玉米多胺氧化酶晶体。这些晶体属于六方空间群P6122(或P6522),晶胞参数为a = b = 184.6 Å,c = 280.9 Å。在同步辐射源上已收集到分辨率为2.7 Å的天然数据集。

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