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Crystallization of Chicken Egg-White Lysozyme from Ammonium SulfateChicken egg-white lysozyme was crystallized from ammonium sulfate over the pH range 4.0-7.8, with protein concentrations from 100 to 150 mg/ml. Crystals were obtained by vapor-diffusion or batch-crystallization methods. The protein crystallized in two morphologies with an apparent morphology dependence on temperature and protein concentration. In general, tetragonal crystals could be grown by lowering the protein concentration or temperature. Increasing the temperature or protein concentration resulted in the growth of orthorhombic crystals. Representative crystals of each morphology were selected for X-ray analysis. The tetragonal crystals belonged to the P4(sub 3)2(sub 1)2 space group with crystals grown at ph 4.4 having unit-cell dimensions of a = b = 78.7 1, c=38.6 A and diffracting to beyond 2.0 A. The orthorhombic crystals, grown at pH 4.8, were of space group P2(sub 1)2(sub 1)2 and had unit-cell dimensions of a = 30.51, b = 56.51 and c = 73.62 A.
Document ID
19990008036
Acquisition Source
Marshall Space Flight Center
Document Type
Reprint (Version printed in journal)
Authors
Forsythe, Elizabeth L.
(Universities Space Research Association Huntsville, AL United States)
Snell, Edward H.
(NASA Marshall Space Flight Center Huntsville, AL United States)
Pusey, Marc L.
(NASA Marshall Space Flight Center Huntsville, AL United States)
Date Acquired
August 19, 2013
Publication Date
January 1, 1997
Publication Information
Publication: Acta Crystallographica Section D
Publisher: International Union of Crystallography
Volume: D53
ISSN: 0907-4449
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other

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