Search Results - "Ohlendorf, D.H."

Crystal structure of the superantigen staphylococcal enterotoxin type A by Schad, E.M., Zaitseva, I., Zaitsev, V.N., Dohlsten, M., Kalland, T., Schlievert, P.M., Ohlendorf, D.H., Svensson, L.A.

“…Staphylococcal enterotoxins are prototype superantigens characterized by their ability to bind to major histocompatibility complex (MHC) class II molecules and…”
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Determination of the quaternary structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa by Ohlendorf, D H, Weber, P C, Lipscomb, J D

“…A 2.5 A resolution data set has been collected for crystals of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Analysis of the data using the…”
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Structural Origins of High-Affinity Biotin Binding to Streptavidin by Weber, Patricia C., Ohlendorf, D. H., Wendoloski, J. J., Salemme, F. R.

“…The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an…”
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A study of protocatechuate 3,4-dioxygenase mutants and substrate interactions by Hoeft, R.D., Shi, K., Gu, Z.-Y., Brown, C.K., Digre, J., Earhart, C.A., Ohlendorf, D.H.

“…Abstract only…”
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Activities and structure of beta toxin by Huseby, M.J., Shi, K., Kruse, A.C., Schlievert, P.M., Ohlendorf, D.H., Earhart, C.A.

“…Abstract only…”
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Protein Crystal Growth in Microgravity by DeLucas, Lawrence J., Smith, Craig D., Smith, H. Wilson, Vijay-Kumar, Senadhi, Senadhi, Shobha E., Ealick, Steven E., Carter, Daniel C., Snyder, Robert S., Weber, Patricia C., Salemme, F. Raymond, Ohlendorf, D. H., Einspahr, H. M., Clancy, L. L., Navia, Manuel A., McKeever, Brian M., Nagabhushan, T. L., Nelson, George, McPherson, A., Koszelak, S., Taylor, G., Stammers, D., Powell, K., Darby, G., Bugg, Charles E.

“…The crystals of most proteins or other biological macromolecules are poorly ordered and diffract to lower resolutions than those observed for most crystals of…”
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DNA-Binding Proteins by Takeda, Y., Ohlendorf, D. H., Anderson, W. F., Matthews, B. W.

“…The structures of three proteins that regulate gene expression have been determined recently and suggest how these proteins may bind to their specific…”
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molecular basis of DNA-protein recognition inferred from the structure of cro repressor by Ohlendorf, D.H, Anderson, W.F, Fisher, R.G, Takeda, Y, Matthews, B.W

“…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…”
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Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda by Ohlendorf, D H, Anderson, W F, Lewis, M, Pabo, C O, Matthews, B W

“…The three-dimensional structures of cro repressor protein and of the amino-terminal domain of lambda repressor protein, both from bacteriophage lambda, are…”
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Lipid and polypeptide components of the crystalline yolk system from Xenopus laevis by Ohlendorf, D H, Barbarash, G R, Trout, A, Kent, C, Banaszak, L J

“…The polypeptide and lipid components of the crystallinelipoprotein-phosphoprotein from the yolk system of Xenopus laevis are described. This lipoprotein…”
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Cro repressor protein and its interaction with DNA by Matthews, B W, Ohlendorf, D H, Anderson, W F, Fisher, R G, Takeda, Y

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Crystalline lipoprotein-phosphoprotein complex in oocytes from Xenopus laevis: determination of lattice parameters by x-ray crystallography and electron microscopy by Ohlendorf, D H, Collins, M L, Puronen, E O, Banaszak, L J

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