Crystallization and preliminary X-ray structure determination of Lupinus luteus PR10 protein

被引：17

作者：

Biesiadka, J

Sikorski, MM

Bujacz, G

Jaskólski, M

机构：

[1] Polish Acad Sci, Inst Bioorgan Chem, PL-61704 Poznan, Poland

[2] Lodz Tech Univ, Inst Tech Biochem, PL-90924 Lodz, Poland

[3] Adam Mickiewicz Univ, Fac Chem, Dept Crystallog, Poznan, Poland

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444999011221

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The pathogenesis-related protein of the PR10 class from Lupinus luteus (yellow lupin), L1PR10.1A, is constitutively expressed in roots. It is also accumulated in leaves treated with a suspension of pathogenic bacteria as a response to stress. Recombinant yellow-lupin L1PR10.1A protein has been overexpressed in Escherichia coli as a fusion product with maltose-binding protein. L1PR10.1A crystallizes in the orthorhombic P2(1)2(1)2(1) space group and the crystals diffract to 2.45 Angstrom resolution. The structure has been solved by molecular replacement, using the structure of a birch-pollen allergen protein as a model.

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页码：1925 / 1927

页数：3

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