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

Xavier Robert, Tine E. Gottschalk, Richard Haser, Birte Svensson, Nushin Aghajari

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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.
Original languageEnglish
JournalActa Crystallographica. Section D: Biological Crystallography
Volume58
Pages (from-to)683-686
ISSN0907-4449
Publication statusPublished - 2002
Externally publishedYes

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