Journal of Molecular Biology
Volume 126, Issue 2, 5 December 1978, Pages 159-183
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Crystals of modified fibrinogen: Size, shape and packing of molecules

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Abstract

We have produced several new macroscopic crystal forms and a variety of microcrystals from modified flbrinogens. Bovine and rabbit flbrinogens crystallize after limited digestion by a bacterial protease or α-chymotrypsin. The fibrinogens making up these crystals are largely intact and highly clottable. Tentative molecular packing arrangements for two crystal forms have been deduced. The crystal morphology and cleavage planes were used in this analysis. The characteristic α-helical coiled-coil reflections arid spikes of intensity in certain directions in the crystal X-ray patterns serve as markers for the orientation of the fibrinogen molecules. Changes that occur in one of the forms during preparation for electron microscopy, as shown by comparison with X-ray experiments on crystals in various stains and solvents, support this packing model. These studies provide preliminary evidence that fibrinogen is about 450 Å in length and that the molecules bond end-to-end to form filaments making up the crystals.

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      Bovine fibrinogen was first crystallized after proteolytic removal of C-terminal portions of the Aα chains with a bacterial enzyme possessing unique specificity (Tooney and Cohen, 1972, 1974). Both crystals and microcrystals of this modified fibrinogen were examined by electron microscopy and analyzed to provide information about fibrinogen structure and the molecular packing in fibrin (Cohen et al., 1983; Weisel et al., 1978, 1981). These crystal forms are unusual in that they are made up of end-to-end bonded molecules that form flexible filaments.

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    This research was supported by National Institutes of Health grant AM17346 to one of us (C. C.).

    Present address: National Center for Atmospheric Research, Boulder, Col. 80307, U.S.A.

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