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- W2142103207 abstract "Two proteins that act as α-amylase inhibitors, Haim I and Paim I, were crystallized and preliminary X-ray diffraction studies on them were carried out. We also sequenced Haim I prepared from Streptomyces griseosporeus YM-25 and confirmed that it is composed of 78 amino acid residues. Crystals of Haim I were grown from ammonium sulfate solution mixed with ethanol by the vapor diffusion technique. The crystals grew as hexagonal bipyramids and diffracted X-rays beyond 2.0 A resolution. They belong to the space group P6122 (or P6622) with unit cell dimensions of a=b=36.7 A, c=192.4 Å, and contain one molecule per asymmetric unit. Paim I, a protein of 39 amino acid residues produced by Streptomyces corchorusii, was crystallized under similar conditions to Haim I. The crystals diffracted X-rays beyond 2.5 Å. They belong to the space group P41212 (or P43212) with unit cell dimensions of a=b=65.4 Å, c=96.1 Å, and contain three molecules per asymmetric unit." @default.
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- W2142103207 date "1994-01-01" @default.
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- W2142103207 title "Crystallization and Preliminary Crystallographic Data of the α-Amylase Inhibitors, Haim I and Paim I" @default.
- W2142103207 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a124295" @default.
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