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Protein crystal growth rates determined by time lapse microphotography

Published on Mar 1, 1991in Journal of Crystal Growth 1.57
· DOI :10.1016/0022-0248(91)90882-6
Stanley Koszelak12
Estimated H-index: 12
(UCR: University of California, Riverside),
David Martin33
Estimated H-index: 33
(UCR: University of California, Riverside)
+ 1 AuthorsAlexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
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Abstract
Abstract Time lapse video microscopy has been used to make qualitative observations of the events that transpire during normal and abnormal protein crystal growth. It has also been used to make quantitative assessments of growth rates for a variety of different protein crystals. From analyses of the growth rates, we have estimated that in the most rapidly growing crystals we have recorded, as many as 20 layers of protein molecules add to a single crystal face per second. In the slowest cases of growth, such as virus crystals, a minute or more may be required for addition of a single layer. In almost all cases, growth was linear over nearly the entire period of growth before leveling near growth termination. We present here a small but typical sample of the results obtained using the time lapse video microscopy technique.
  • References (12)
  • Citations (21)
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References12
Newest
Published on Sep 1, 1989in Journal of Molecular Biology 5.07
Stanley Koszelak12
Estimated H-index: 12
(UCR: University of California, Riverside),
James Allan Dodds1
Estimated H-index: 1
(UCR: University of California, Riverside),
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
Abstract Satellite tobacco mosaic virus (STMV), a small T = 1 icosahedral plant virus, has been crystallized in a form suitable for high-resolution X-ray diffraction analysis. The crystals, which diffract to better than 2.5 A resolution, are of space group I 222 and have unit cell dimensions of a = 176 A , b = 192 A and c = 205 A . The centers of the virus particles occupy 222 symmetry points in the unit cell and one quarter of the virus particle constitutes the asymmetric unit, which is therefo...
Published on Jun 1, 1989in Journal of Biomolecular Structure & Dynamics 3.31
Joseph D. Ng3
Estimated H-index: 3
(UCR: University of California, Riverside),
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
Abstract A proteolytically modified form of the Escherichia coli single-stranded DNA-Binding protein (SSB) has been crystallized from 15% saturated sodium citrate. Crystals as large as 1.0mm × 0.3mm × 0.2mm were obtained and these diffract beyond 3A resolution. X-ray photographic analysis demonstrated a rhombohedral unit cell of space group R3 with an equivalent triple centered hexagonal unit cell having dimensions of a = b = 62.9 A and c = 264.3A. These crystals were judged to be adequate for a...
Published on Jul 1, 1988in Journal of Crystal Growth 1.57
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside),
Paul J. Shlichta10
Estimated H-index: 10
(California Institute of Technology)
Abstract Fifty different mineral samples were tested as potential heterogeneous or epitaxial nucleants for four commonly crystallized proteins. It was found, using conventional protein crystallization techniques, that for each protein there was a set of mineral substrates that promoted nucleation of crystals at lower critical levels of supersaturation then required for spontaneous growth. In at least one case, the growth of lysozyme on the mineral apophyllite, it was shown by lattice analysis an...
Published on Jul 1, 1988in Journal of Crystal Growth 1.57
Stanley Koszelak12
Estimated H-index: 12
(UCR: University of California, Riverside),
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
Abstract A time lapse video color recorder (VCR) interfaced to a color video camera mounted on a light microscope was used to observe and record the growth of three protein crystals: lysozyme, canavalin, and a fungal protease. The studies produced a number of interesting observations regarding the formation of crystal habit, crystal aggregates, and crystal polymorphs. It further provided a simple and easy means for the measurement of growth rates. The system is described here along with a brief ...
Published on Jan 22, 1988in Science 41.04
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside),
Paul J. Shlichta10
Estimated H-index: 10
(California Institute of Technology)
Fifty different mineral samples were tested as potential heterogeneous or epitaxial nucleants for four commonly crystallized proteins. It was found, by conventional protein crystallization techniques, that for each protein there was a set of mineral substrates that promoted nucleation of crystals at lower critical levels of supersaturation than required for spontaneous growth. Numerous examples, involving all four proteins, were observed of modification of crystal habit and, in some cases, unit ...
Published on Feb 5, 1987in Journal of Biological Chemistry
A McPherson1
Estimated H-index: 1
,
C N Hankins1
Estimated H-index: 1
,
L Shannon1
Estimated H-index: 1
Abstract The Japanese Pogada Tree (Sophora japonica) contains at least four distinct lectins distributed among seeds, bark, and leaf tissues of the plant. All of these lectins are N-acetylgalactosamine-specific, have molecular weights of about 130,000, are glycoproteins and possess substantial sequence homology. However, they are products of distinct genes. We have crystallized Sophora lectins from bark, seeds, and two different lectins from leaves. Multiple crystal forms of each variety have be...
Published on Aug 1, 1986in Journal of Crystal Growth 1.57
Marc L. Pusey26
Estimated H-index: 26
(MSFC: Marshall Space Flight Center),
Robert J. Naumann8
Estimated H-index: 8
(MSFC: Marshall Space Flight Center)
Abstract A method has been devised for immobilizing protein crystals in small volumes under defined conditions in order to determine growth rates on various faces. Using this method, we have investigated the growth kinetics of the [110] face of tetragonal hens egg white lysozyme crystals at varying degrees of bulk supersaturation. The growth rate data were analyzed using a simple convective-diffusive model to determine an empirical relationship between growth rate and local supersaturation at th...
Published on Oct 1, 1982in Plant Physiology 6.30
Stephanie Campbell Smith2
Estimated H-index: 2
,
Stephen Johnson3
Estimated H-index: 3
+ 1 AuthorsAlexander McPherson53
Estimated H-index: 53
The structure of canavalin, a jack bean ( Canavalis ensiformis ) protein homologous to phaseolin, the major seed storage protein of Phaseolus vulgaris , has been investigated by x-ray crystallography and found to be a hexamer composed of three identical pairs of similar but nonidentical subunits related by a perfect 3-fold axis and pseudo dyad axes (strict C 3 and pseudo D 3 ). One member of each pair of subunits is derived from the amino terminal half of a precursor polypeptide of molecular wei...
Published on Jan 1, 1982
Alexander McPherson53
Estimated H-index: 53
A complete guide to techniques and procedures for the preparation of proteins for crystallographic studies. Describes methods for protein crystallization; formation of isomorphous heavy atoms; x-ray diffraction and analysis; and photographic and computerbased data collection methods and instrumentation.
Published on Nov 10, 1980in Journal of Biological Chemistry
A McPherson1
Estimated H-index: 1
Abstract The structure of the jack bean (Canavalia ensiformis) protein canavalin, which forms the classical vicillin fraction of the seed protein in this species, has been determined for the rhombohedral (R3) crystal form to 3.0-A resolution. X-ray diffraction data were collected by the screened precession method for the native protein and five heavy atom derivatives and the phases were determined by conventional isomorphous replacement. The electron density map thus obtained, and a molecularly ...
Cited By21
Newest
Published on Oct 1, 2018in Protein Science 2.42
Renee J. Arias1
Estimated H-index: 1
(California Institute of Technology),
Jens T. Kaiser15
Estimated H-index: 15
(California Institute of Technology),
Douglas C. Rees74
Estimated H-index: 74
(California Institute of Technology)
Published on Nov 1, 2015
Alexander McPherson53
Estimated H-index: 53
,
Lawrence J. DeLucas24
Estimated H-index: 24
Published on Jul 10, 2013
Dimitra Nikolaidi (University of Nottingham)
Structure elucidation of a macromolecule can lead to the determination of its function. In the case of proteins, knowledge of their three-dimensional structure can be utilised in the identification of active site(s) and consequently in rational drug design. Commonly, X-ray crystallography is implemented on a high quality single crystal of the target macromolecule, in order to elucidate its structure. Moreover, crystallised protein molecules may remain active which can then be used in controlled ...
Published on Jan 1, 2004
J.M. García-Ruiz1
Estimated H-index: 1
(CSIC: Spanish National Research Council),
F. Otálora1
Estimated H-index: 1
(CSIC: Spanish National Research Council)
Publisher Summary This chapter reviews the techniques used to characterize macromolecular crystals. It discusses the relationship between the growth conditions and the crystal quality. The macromolecular crystals are grown according to the classical crystal growth mechanisms. They contain all the crystalline defects found in crystals of small molecules. Biological macromolecules such as proteins, carbohydrates, nucleic acids and viruses form crystals. The crystallization of these large molecules...
Published on Jan 1, 1999in Journal of Crystal Growth 1.57
Alexander McPherson53
Estimated H-index: 53
(UCI: University of California, Irvine),
Alexander J. Malkin22
Estimated H-index: 22
(UCI: University of California, Irvine)
+ 5 AuthorsGreg Lawson1
Estimated H-index: 1
Atomic force microscopy (AFM) investigations have revealed that macromolecular crystals, during their growth, incorporate an extensive array of impurities. These vary from individual molecules to large particles, and microcrystals in the micron size range. AFM, along with X-ray topology, has further shown that the density of defects and faults in most macromolecular crystals is very high in comparison with conventional crystals. The high defect density is a consequence of the incorporation of im...
Published on Jul 1, 1997in Journal of Crystal Growth 1.57
Juan Manuel García-Ruiz32
Estimated H-index: 32
(CSIC: Spanish National Research Council),
Abel Moreno2
Estimated H-index: 2
(CSIC: Spanish National Research Council)
The growth of single crystals of tetragonal HEW lysozyme and thaumatin I into glass capillaries was monitored by time lapse video-microscopy. The crystals were obtained by unidirectional transport of the precipitating agent through capillaries of internal diameter ranging from 0.2 to 1.2 mm, using the gel acupuncture technique. For crystals growing from true protein solutions, the measured average growth rates varies with capillary diameter from 1.7 to 3.7 A/s for thaumatin and from 2.8 to 22 A/...
Published on Oct 1, 1996in Journal of Crystal Growth 1.57
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside),
A Malkin18
Estimated H-index: 18
(UCR: University of California, Riverside)
+ 1 AuthorsStanley Koszelak12
Estimated H-index: 12
(UCR: University of California, Riverside)
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...
Published on Aug 1, 1996in Quarterly Reviews of Biophysics 6.64
Naomi E. Chayen33
Estimated H-index: 33
(Imperial College London),
Titus J. Boggon5
Estimated H-index: 5
(University of Manchester)
+ 16 AuthorsMark R. Peterson6
Estimated H-index: 6
(University of Manchester)
Macromolecular X-ray crystallography underpins the vigorous field of structural molecular biology having yielded many protein, nucleic acid and virus structures in fine detail. The understanding of the recognition by these macromolecules, as receptors, of their cognate ligands involves the detailed study of the structural chemistry of their molecular interactions. Also these structural details underpin the rational design of novel inhibitors in modern drug discovery in the pharmaceutical industr...
Published on Feb 1, 1996in Proteins
A Malkin18
Estimated H-index: 18
(UCR: University of California, Riverside),
Yurii G. Kuznetsov4
Estimated H-index: 4
(UCR: University of California, Riverside),
Alexander McPherson53
Estimated H-index: 53
(UCR: University of California, Riverside)
Published on Dec 1, 1993in Advances in Colloid and Interface Science 8.24
Yannis Georgalis17
Estimated H-index: 17
(FU: Free University of Berlin),
Wolfram Saenger73
Estimated H-index: 73
(FU: Free University of Berlin)
Abstract X-ray diffraction is one of the most important methods for determining the three-dimensional structure of biological macromolecules. However, obtaining biological crystals is a lengthy and painstaking endeavour. Therefore, no universal recipes exist ;thus the field of protein crystallization can be judged as highly empirical. Hen-egg white lysozyme has served as a prototype to study the early stages of protein crystallization. Crystallization is initiated by addition of simple salts and...