Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2

Birte Svensson, Richard M. Gibson, Richard Haser, Jean Pierre Astier

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

alpha-Amylase isozymes 1 and 2 isolated from germinated barley seeds have been crystallized by the hanging- or sitting-drop vapor diffusion technique. Crystals of alpha-amylase 2 suitable for x-ray diffraction analysis were grown at pH 6.7 and 22 degrees C from a solution of 1 mM calcium chloride, 10 mM MES, and 16% saturated ammonium sulfate. The space group is trigonal P3121 (or P3221) with unit cell dimensions a = b = 135.20 A, c = 79.63 A, and probably two molecules per asymmetric unit.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume262
Pages (from-to)13682-12684
ISSN0021-9258
Publication statusPublished - 1987
Externally publishedYes

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