Sukumar, N and Biswal, BK and Vijayan, M (1999) Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant. In: Acta Crystallographica Section D: Biological Crystallography, 55 (4). pp. 934-937.
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The structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant have been solved and refined at 1.9 and 2.0 \AA resolution, respectively. A comparison of the native structure with those of crystals grown at acidic pH does not show any systematic pH-dependent difference in the molecular geometry. The conformations, mutual orientation and interactions of the catalytic residues Glu35 and Asp52 also remain unchanged. However, comparison between the native and low-humidity forms in the orthorhombic form show that the changes in molecular geometry which accompany the water-mediated transformation to the low-humidity form are more pronounced in the C-terminal residues than in the other regions of the molecule. During the transformation from the native to the low-humidity form, the locations of only about half the water molecules in the hydration shell remain unchanged, but the hydration shell as a whole moves along with the protein molecule.
|Item Type:||Journal Article|
|Additional Information:||Copyright og this article belongs to International Union of Crystallography.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||04 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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