ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Pig pancreatic α-amylase (PPA, E.C. 3.2. 1. 17, 496 amino-acid residues) has been crystallized as a complex with a lectin-like inhibitor from bean Phaseolus vulgaris (224 amino-acid residues for the inhibitor monomer). The hanging-drop vapour-diffusion method was used to grow crystals from solutions containing 2-methyl-2,4-pentanediol as precipitant. The crystals belong to monoclinic space group C2 with a = 152.5, b = 80.3, c = 68.8 Å, β = 91.4 and diffract to 2.9 Å resolution. A molecular-replacement solution of the structure has been obtained using the refined PPA and LoLl (Lathyrus ochrus isolectin I) atomic coordinates as starting models. Low-resolution refinement of the model is underway. The analysis reveals that the functional inhibitor molecule is dimeric and interacts with two molecules of enzyme.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444995016064
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