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Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):69-72.

Well ordered crystals of a short-chain alcohol dehydrogenase from Drosophila lebanonensis: re-evaluation of the crystallographic data and rotation-function analysis.

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Karolinska Institute, NOVUM, Center for Structural Biochemistry, Huddinge, Sweden.


Alcohol dehydrogenase prepared from Drosophila lebanonensis yields well ordered plate-like crystals which diffract to better than 2.3 A resolution. The crystals belong to space group P2(1) of the monoclinic system; the unit-cell dimensions are a = 65.25, b = 55.77, c = 70.02 A, alpha = 90, beta = 107.08, gamma = 90 degrees. The asymmetric unit of the crystal cell is most probably occupied by a dimer, corresponding to a packing density of 2.15 A(3) Da-L. The orientation of the non-crystallographic twofold symmetry axes is determined by analysis of a self-rotation function calculated with native intensity data.


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