Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds.

Robert X; Gottschalk TE; Haser RSvensson BAghajari N

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds.

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Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds.

机译：表达、纯化和初步的晶体阿尔法淀粉酶同工酶的研究1从大麦种子。

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The germinating barley seed contains two major alpha-amylase isozyme families, AMY1 and AMY2, involved in starch degradation to provide energy used by the plant embryo for growth. Many years of difficulty in growing three-dimensional crystals of natural AMY1 have now been overcome by a nonapeptide truncation of the enzyme C-terminus. The truncated enzyme was overexpressed in Pichia pastoris, purified and crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as precipitant and 2-propanol as an additive. Crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 88.36, b = 72.82, c = 61.74 A and one molecule per asymmetric unit.

机译：发芽大麦种子包含两个主要的阿尔法淀粉酶同工酶家族,AMY1 AMY2,参与淀粉降解提供能量所使用的植物胚胎的增长。越来越多的三维中所遇到的困难水晶的自然AMY1现在已经克服由一个九肽酶的截断糖基。在毕赤酵母属pastoris,纯化和结晶的悬滴vapour-diffusion方法利用聚乙二醇8000沉淀剂和丙胺作为一种添加剂。晶体属斜方晶系的空间群P2(1) 2(1) 2,晶胞参数= 88.36,b = 72.82, c = 61.74,每一个分子不对称单元。

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《Acta crystallographica.Section D. Biological crystallography》 |2002年第4期|683-686|共4页
作者
Robert X; Gottschalk TE; Haser RSvensson BAghajari N;
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作者单位

Institut de Biologie et Chimie des Proteines, Laboratoire de Bio-Cristallographie CNRS-UMR 5086, 69367 Lyon CEDEX 07, France.;

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正文语种英语
中图分类化学;
关键词
Isoenzymes; alpha-Amylases; HordeumBarleyKomagataella pastorismacrogol 8000Isopropyl Alcohol;

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Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds.

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