| The Yeast Spindle Pole Body Is Assembled around a Central Crystal of Spc42p Cell, Volume 89, Issue 7, 27 June 1997, Pages 1077-1086 Esther Bullitt, Michael P. Rout, John V. Kilmartin and Christopher W. Akey Summary The spindle pole body (SPB) is the microtubule organizing center (MTOC) in the yeast Saccharomyces that plays a pivotal role in such diverse processes as mitosis, budding, and mating. We have used cryoelectron microscopy and image processing to study the structure of isolated diploid SPBs. We show that SPBs are present in two lateral-size classes, sharing a similar vertical architecture comprised of six major layers. Tomographic reconstructions of heparin-stripped SPBs reveal a central hexagonally packed layer. Overexpression of Spc42p results in the growth of a similar layer, forming a crystal that encircles the SPB. Hence, the SPB is an MTOC that utilizes crystallographic packing of subunits in its construction. Summary | Full Text | PDF (471 kb) |
| Physical Detwinning of Hemihedrally Twinned Hexagonal Crystals of Bacteriorhodopsin Biophysical Journal, Volume 87, Issue 5, 1 November 2004, Pages 3608-3613 Rouslan Efremov, Rouslan Moukhametzianov, Georg Büldt and Valentin Gordeliy Abstract Hexagonal crystals of the membrane protein bacteriorhodopsin of space group P6 grown in lipidic cubic phase are twinned hemihedrally. It was shown that slow changes of salt concentration in the mother liquor lead to a split of crystals so that the split parts preserved high diffraction quality. Analysis of diffraction data from split crystals by Yeates statistic and Britton plot showed that the split parts are free of twinning. It is concluded that crystals of bacteriorhodopsin are composed of several macroscopic twinning domains with sizes comparable to the original crystal. The appearance of twinning domains during crystal growth and the mechanism of splitting are discussed. Abstract | Full Text | PDF (204 kb) |
| X-Ray Diffraction Characterization of the Dense Phases Formed by Nucleosome Core Particles Biophysical Journal, Volume 84, Issue 4, 1 April 2003, Pages 2570-2584 Stéphanie Mangenot, Amélie Leforestier, Dominique Durand and Françoise Livolant Abstract Multiple dense phases of nucleosome core particles (NCPs) were formed in controlled ionic conditions (15–160mM monovalent salt, no divalent ions), under osmotic pressures ranging from 4.7×10 to 2.35×10 Pa. We present here the x-ray diffraction analysis of these phases. In the lamello-columnar phase obtained at low salt concentration (<25mM), NCPs stack into columns that align to form bilayers, kept separated from one another by a layer of solvent. NCPs form a monoclinic lattice in the plane of the bilayer. For high salt concentration (>50mM), NCPs order into either a two-dimensional columnar hexagonal phase or into three-dimensional orthorhombic (quasi-hexagonal) crystals. The lamellar and hexagonal (or quasi-hexagonal) organizations coexist in the intermediate salt range; their demixing requires a long time. For an applied pressure =4.7 10 Pa, the calculated NCPs concentration ranges from ∼280 to 320 mg/ml in the lamello-columnar phase to 495 to 585 mg/ml in the three-dimensional orthorhombic phase. These concentrations cover the concentration of the living cell. Abstract | Full Text | PDF (558 kb) |
Copyright © 1980 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 32, Issue 2, 851-856, 1 November 1980
doi:10.1016/S0006-3495(80)85020-X
Research Article
K.H. Downing and R.M. Glaeser
Crystals of DNA have been grown in a form suitable for study by electron diffraction and electron microscopy. Preliminary electron diffraction patterns of any type that have been obtained from single crystals of highly polymerized DNA. The patterns, obtained from frozen, hydrated crystals with the beam approximately parallel to the DNA strand axis, show a hexagonal geometrical arrangement with a (1,0) Bragg spacing of 23.1 A.