These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification, crystallization and preliminary X-ray crystallographic study of alpha-amylase from Bacillus stearothermophilus.
    Author: Suvd D, Takase K, Fujimoto Z, Matsumura M, Mizuno H.
    Journal: Acta Crystallogr D Biol Crystallogr; 2000 Feb; 56(Pt 2):200-2. PubMed ID: 10666605.
    Abstract:
    A recombinant alpha-amylase from Bacillus stearothermophilus was found to be produced as several isoforms arising from different N--terminal processing. Some of those isoforms were purified to homogeneity and crystallized at 293 K using the hanging-drop vapour-diffusion method under the following conditions: 35 mM sodium acetate (pH 4.6), 6.25%(v/v) 2-propanol, in the presence of 1.23%(w/v) acarbose (a pseudo-oligosaccharide inhibitor) in the drop. The crystals diffracted beyond 2.0 A resolution using synchrotron radiation at the Photon Factory, Tsukuba. They belong to the monoclinic space group P2(1), with unit-cell parameters a = 53.7 (2), b = 92.9 (4), c = 53.2 (2) A, beta = 109.4 (1) degrees.
    [Abstract] [Full Text] [Related] [New Search]