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Volume 271, Number 46, Issue of November 15, 1996 pp. 28731-28733
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
Crystallization and Preliminary X-ray Analysis of a Low Density Lipoprotein from Human Plasma

(Received for publication, August 5, 1996)

Ruth Prassl , John M. Chapman ^§ , Fabienne Nigon ^§ , Margit Sara ^¶ , Susanne Eschenburg , Christian Betzel , Ajay Saxena and Peter Laggner

From the  Institute of Biophysics and X-ray Structure Research, Austrian Academy of Sciences, A-8010 Graz, Austria, ^§ INSERM Unite 321, F-75651 Paris, France, the ^¶ Centre for Ultrastructure Research, Agricultural University, A-1010 Vienna, Austria, and the  EMBL-Outstation at DESY, D-22603 Hamburg, Federal Republic of Germany

Single crystals of human plasma low density lipoprotein (LDL), the major transport vehicle for cholesterol in blood, have been produced with a view to analysis of the three-dimensional structure by x-ray crystallography. Crystals with dimensions of approximately 200 × 100 × 50 µm have been reproducibly obtained from highly homogeneous LDL particle subspecies, isolated in the density ranges d = 1.0271-1.0297 g/ml and d = 1.0297-1.0327 g/ml. Electron microscopic imaging of ultrathin-sectioned preparations of the crystals confirmed the existence of a regular, quasihexagonal arrangement of spherical particles of approximately 18 nm in diameter, thereby resembling the dimensions characteristic of LDL after dehydration and fixation. X-ray diffraction with synchrotron radiation under cryogenic conditions revealed the presence of well resolved diffraction spots, to a resolution of about 29 Å. The diffraction patterns are indexed in terms of a triclinic lattice with unit cell dimensions of a = 16.1 nm, b = 39.0 nm, c = 43.9 nm;  = 96.2°,  = 92.1°,  = 102°, and with space group P1.

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