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  • 1
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    Structural origins of high-affinity biotin binding to streptavidin (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-06
    Description: The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, P C -- Ohlendorf, D H -- Wendoloski, J J -- Salemme, F R -- New York, N.Y. -- Science. 1989 Jan 6;243(4887):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research & Development Department, E. I. du Pont de Neumours and Company, Inc., Wilmington, DE 19880-0228.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911722" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Binding Sites ; Biotin/*metabolism ; Macromolecular Substances ; Models, Molecular ; Protein Conformation ; Streptavidin ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    DNA-binding proteins (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-09-09
    Description: The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific recognition sites on the DNA. One protein (Cro) is a repressor of gene expression, the second (CAP) usually stimulates gene expression, and the third (lambda repressor) can act as either a repressor or an activator. The three proteins contain a substructure consisting of two consecutive alpha helices that is virtually identical in each case. Structural and amino acid sequence comparisons suggest that this bihelical fold occurs in a number of proteins that regulate gene expression, and is an intrinsic part of the DNA-protein recognition event. The modes of repression and activation by Cro and lambda repressor are understood reasonably well, but the mode of action of CAP is still unclear.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeda, Y -- Ohlendorf, D H -- Anderson, W F -- Matthews, B W -- GM20066/GM/NIGMS NIH HHS/ -- GM28138/GM/NIGMS NIH HHS/ -- GM30894/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Sep 9;221(4615):1020-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6308768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; *DNA Helicases ; DNA-Binding Proteins ; Escherichia coli/genetics ; Gene Expression Regulation ; Models, Chemical ; Protein Conformation
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    Acuracy of refined protein structures. II. Comparison of four independently refined models of human interleukin 1β (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 808-812 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: To assess the accuracy of refined structures, a comparison was made using independently determined structures of the same protein in the same crystal form. The models were re-refined against a common data set to minimize the effects of different data and different refinement protocols. The process did not converge to a single model. Rather the structures differed from each other by 0.84 Å which was roughly three times that predicted by a Luzzati analysis [Luzzati (1952). Acta Cryst. 5, 802–810]. The individual structures are equally valid and at least partially independent as evidenced by a reduction of the R factor by 0.013 when a simple linear combination is used. Only 29 solvent molecules were common to all four models.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994002659
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  • 4
    Electronic Resource
    Electronic Resource
    An oscillation data collection system for high-resolution protein crystallography (1981)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 37 (1981), S. 701-710 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: An oscillation data collection system for protein crystallography is described. The system consists of a modified Enraf-Nonius precession camera with cylindrical cassette, and stepping motor driven by a flexible microprocessor control system. The X-ray source is graphite-monochromatized radiation from an Elliott GX-21 rotating-anode generator run at 5.5 kW on a focal spot measuring 0.5 × 5.0 mm. The potential advantages of using a relatively large focal spot in conjunction with a graphite monochromator are discussed. Conditions for optimum collimation and X-ray intensity are considered, and it is shown that appropriately designed collimators with adjustable apertures can have substantial advantages over commercially available pinhole collimators. The oscillation films are processed by a procedure based on that of Rossmann [J. Appl. Cryst. (1979), 12, 225-238]. Determination of the initial alignment of the film is facilitated by a pair of reference pins incorporated in the cylindrical cassette. These pins ensure that the position of the film in the cassette is known, and avoid the need for fiducial marks. The crystal alignment and film measurement technique is fully automatic, requiring no prior input other than the approximate starting orientation of the crystal, the approximate unit-cell dimensions, and the angular oscillation range. An alternative method for the determination of crystal orientation is proposed which has been found to be somewhat superior to that of Rossmann, especially for smaller unit cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739481001587
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  • 5
    Electronic Resource
    Electronic Resource
    Structural Studies of Protein-Nucleic Acid Interactions (1983)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 12 (1983), S. 259-284 
    Details
    ISSN: 0084-6589
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bb.12.060183.001355
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  • 6
    Electronic Resource
    Electronic Resource
    The molecular basis of DNA–protein recognition inferred from the structure of cro repressor (1982)
    [s.l.] : Nature Publishing Group
    Nature 298 (1982), S. 718-723 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Recognition by cro repressor protein of its specific DNA binding sites appears to occur via multidentate hydrogen bonds between amino acid side chains of the protein and base-pair atoms in the major groove of right-handed B-form DNA. Most of the sequence-specific interactions between cro and DNA, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/298718a0
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  • 7
    Electronic Resource
    Electronic Resource
    Structure and assembly of protocatechuate 3,4-dioxygenase (1988)
    [s.l.] : Nature Publishing Group
    Nature 336 (1988), S. 403-405 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The structure of 3,4-PCD was solved using a combination of isomorphous replacement and molecular averaging to produce the map in Fig. 1. This map shows continuous electron density for both chains and accounts for all but the first three and last two residues of the ft chain. The course of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/336403a0
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  • 8
    Electronic Resource
    Electronic Resource
    The use of an imaging proportional counter in macromolecular crystallography (1987)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 20 (1987), S. 383-387 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: A multiwire proportional chamber known as an imaging proportional counter has been used to collect X-ray intensity data for the determination of several structures by molecular replacement or difference Fourier analysis and has provided data for numerous other macromolecular crystallographic projects. Results obtained with an imaging proportional counter mounted on a rotating-anode X-ray generator indicate that the detector produces accurate intensity information and that its reliability is high.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889887086436
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  • 9
    Electronic Resource
    Electronic Resource
    Visualization software for X-ray diffraction data from area detectors (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 24 (1991), S. 64-66 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Computational tools for examining data obtained from area detectors are described. These programs use a raster terminal as a frame buffer to display images helpful in the analysis of X-ray diffraction data frames and to display images diagnostic of potential problems during data collection or processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889890006616
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  • 10
    Electronic Resource
    Electronic Resource
    Crystallographic refinement of bovine pro-phospholipase A2 at 1.6 Å resolution (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 47 (1991), S. 814-816 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108768191004226
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