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The incorporation of large impurities into virus crystals

Published on Jun 1, 2005in Acta Crystallographica Section D-biological Crystallography3.227
· DOI :10.1107/S0907444904030756
Yu. G. Kuznetsov19
Estimated H-index: 19
(UCI: University of California, Irvine),
Debora L. Makino5
Estimated H-index: 5
(UCI: University of California, Irvine)
+ 1 AuthorsAlexander McPherson51
Estimated H-index: 51
(UCI: University of California, Irvine)
Abstract
Virus crystals can incorporate a wide range of unusual impurities, not possible for conventional crystals, or even most protein crystals because of the large size of their constituent particles. These impurities include anomalous virions, satellite viruses and biological fibers. Examples of several of these unusual impurities are presented here, along with some of the consequences for the crystal lattices. The high solvent content, the forgiving character of the lattice and the plasticity of the virions allow these incorporations to be possible.
  • References (14)
  • Citations (6)
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References14
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#1Yu. G. KuznetsovH-Index: 19
#2J. G. VictoriaH-Index: 2
Last. A. McPhersonH-Index: 9
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Isolated human immunodeficiency virus (HIV) and HIV-infected human lymphocytes in culture have been imaged for the first time by atomic force microscopy (AFM). Purified virus particles spread on glass substrates are roughly spherical, reasonably uniform, though pleomorphic in appearance, and have diameters of about 120 nm. Similar particles are also seen on infected cell surfaces, but morphologies and sizes are considerably more varied, possibly a reflection of the budding process. The surfaces ...
82 CitationsSource
#1Robert W. Lucas (UCI: University of California, Irvine)H-Index: 8
#2Yurii G. Kuznetsov (UCI: University of California, Irvine)H-Index: 17
Last. Alexander McPherson (UCI: University of California, Irvine)H-Index: 51
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Brome mosaic virus (BMV), a T = 3 icosahedral plant virus, can be dissociated into coat protein subunits and subunit oligomers at pH 7.5 in the presence of concentrated salts. We have found that during the course of this treatment the coat protein subunits are cleaved, presumably by plant cell proteases still present in the preparation, between amino acids 35 and 36. The truncated protein subunits will then reorganize into T = 1 icosahedral particles and can be crystallized from sodium malonate....
40 CitationsSource
▪ Abstract Atomic force microscopy (AFM) has been used to study protein, nucleic acid, and virus crystals in situ, in their mother liquors, as they grow. From sequential AFM images taken at brief i...
77 CitationsSource
#1A Malkin (UCR: University of California, Riverside)H-Index: 18
#2Yu. G. Kuznetsov (UCR: University of California, Riverside)H-Index: 19
Last. Alexander McPherson (UCR: University of California, Riverside)H-Index: 51
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Surface morphology, growth and dissolution of crystals of the protein catalase were studied by in situ atomic force microscopy (AFM). Growth of the (001) face of catalase crystals proceeds in alternating patterns by two-dimensional nucleation and successive deposition of two distinctive growth layers, each having a step height equal to half the unit cell parameter. Shapes of two-dimensional nuclei exhibit strong asymmetry due to directional anisotropy in step rates. The shapes of islands on succ...
33 CitationsSource
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#2A Malkin (UCR: University of California, Riverside)H-Index: 18
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Atomic force microscopy (AFM) images at the molecular level have been obtained for a number of different protein and virus crystals. They can be utilized in some special cases to obtain information useful to crystal structure analyses by x-ray diffraction. In particular, questions of space group enantiomer, the packing of molecules within a unit cell, the number of molecules per asymmetric unit, and the dispositions of multiple molecules within the asymmetric unit may be resolved. In addition, b...
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The chemical, mechanical and diffraction properties of crystals grown from solution, as well as their growth kinetics and morphological development, depend very much on the types and concentrations of impurities present in their mother liquor. The situation appears vastly more complicated in the case of macromolecular crystals because of the complex nature of the molecules and the biochemical milieu from which they are derived. An attempt is made here to catalog and characterize these various im...
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Disorder in macromolecular crystals arises from several sources. Among the most important are thermal motion and the inherent mobility of the molecules. These cause statistical misalignment about mean lattice points and structural heterogeneity of the molecules. Defects in the crystal lattice, however, could also significantly affect the resolution and quality of diffraction data collected from some crystals. There is a considerable diversity in the sources of defects found in crystals, such as ...
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: In the course of time-lapse video and atomic force microscopy (AFM) investigations of macromolecular crystal growth, we frequently observed the sedimentation of microcrystals and three-dimensional nuclei onto the surfaces of much larger, growing protein or virus crystals. This was followed by the direct incorporation over time of the smaller crystals into the bulk of the larger crystals. In some cases, clear indications were present that upon absorption of the small crystal onto the surface of...
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Abstract Detailed structures are now available for three plant satellite viruses, satellite tobacco necrosis virus (STNV), satellite tobacco mosaic virus (STMV), and satellite panicum mosaic virus (SPMV). It is, therefore, possible to compare the tertiary structure of viral protein subunits, their quaternary interactions, and the interactions of protein subunits with the RNA genome. This analysis indicates that, in spite of common function and preservation of a “jelly-roll” motif in the protein ...
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For the first time, virus crystal growth dynamics and morphology have been investigated in real time on the nanometer scale. Individual monomers on the (111) face of cubic satellite tobacco mosaic virus (STMV) crystals were resolved and used to determine crystal packing. Growth of STMV proceeded by two- and three-dimensional nucleation to formed ``stacks`` of islands. No dislocations were observed. Small islands provided an estimate of critical radius size and the free energy of the step edge, {...
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