Burk D, Wang Y, Dombroski D, Berghuis A M, Evans S V, Luo Y, Withers S G, Brayer G D
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
J Mol Biol. 1993 Apr 5;230(3):1084-5. doi: 10.1006/jmbi.1993.1221.
Human pancreatic alpha-amylase has been isolated using a glycogen affinity precipitation procedure and crystallized in a form suitable for high resolution three-dimensional X-ray crystallographic analyses. Crystals are of the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 53.04 A, b = 74.80 A and c = 137.34 A, and contain only one protein molecule per asymmetric unit. Diffraction data have been collected and found to extend to 1.6 A resolution. These studies form the basis for elucidating the full atomic structure of human pancreatic alpha-amylase and thereby providing insight into the catalytic mechanism of this enzyme.
人胰腺α-淀粉酶已通过糖原亲和沉淀法分离出来，并以适合高分辨率三维X射线晶体学分析的形式结晶。晶体属于正交空间群P2(1)2(1)2(1)，晶胞参数为a = 53.04 Å，b = 74.80 Å，c = 137.34 Å，每个不对称单元仅包含一个蛋白质分子。已收集到衍射数据，发现其分辨率可达1.6 Å。这些研究为阐明人胰腺α-淀粉酶的完整原子结构奠定了基础，从而有助于深入了解该酶的催化机制。
