Packing analysis of crystalline myosin subfragment-1. Implications for the size and shape of the myosin head
- PMID: 3999137
- DOI: 10.1016/0022-2836(85)90422-x
Packing analysis of crystalline myosin subfragment-1. Implications for the size and shape of the myosin head
Abstract
Crystals of myosin subfragment-1 have been examined by X-ray diffraction and electron microscopy to determine how the molecules pack in the unit cell and to gain preliminary information on the size and shape of the myosin head. Subfragment-1 crystallizes in space group P212121. Analysis of the X-ray diffraction photographs shows that there are eight molecules in the unit cell with two in the asymmetric unit related by a non-crystallographic or local 2-fold axis. It also indicates that in projection down the a axis, two molecules of myosin subfragment-1 lie almost directly on top of one another except for a translation of about 9 A along c. Small crystals were fixed and embedded in the presence of tannic acid, and thin sections were cut perpendicular to each of the three crystallographic axes. Image analysis of micrographs recorded from these sections confirm the packing arrangement deduced from X-ray diffraction, and give the approximate size and shape of the molecule in the crystal lattice. They show that the molecule is at least 160 A long with a maximum thickness of about 60 A, and that it has marked curvature in the unit cell.
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