M R Singleton|S Scaife|D B Wigley - JoVE Visualize

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The EMBO Journal|October 6, 1997

Crystal structure of the site-specific recombinase, XerDH S Subramanya, L K Arciszewska, R A Baker, et al.

Extremophiles : Life Under Extreme Conditions|November 1, 2000

Cloning, expression, and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralisM R Singleton, S J Taylor, J S Parrat, et al.

The EMBO Journal|March 15, 1996

The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallographyR J Lewis, O M Singh, C V Smith, et al.

Journal of Molecular Biology|January 5, 1992

Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolutionD B Wigley, S J Gamblin, J P Turkenburg, et al.

Journal of Molecular Biology|August 5, 1994

Crystallization of inhibitor complexes of an N-terminal 24 kDa fragment of the DNA gyrase B proteinR J Lewis, O M Singh, C V Smith, et al.

Biochemical and Biophysical Research Communications|July 15, 1987

The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenaseK W Hart, A R Clarke, D B Wigley, et al.

Biochemistry|January 23, 1996

Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerasesH S Subramanya, D I Roper, Z Dauter, et al.

Journal of Molecular Biology|February 18, 1994

Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid filmsH Celia, L Hoermann, P Schultz, et al.

Biochimica Et Biophysica Acta|November 5, 1987

The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surfaceD B Wigley, A R Clarke, C R Dunn, et al.

Biochemical and Biophysical Research Communications|January 29, 1988

The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzymeA D Waldman, K W Hart, A R Clarke, et al.

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Showing results (61-70 of 76) with videos related to

Sort By:

Pageof 8

The EMBO Journal|October 6, 1997

Crystal structure of the site-specific recombinase, XerDH S Subramanya, L K Arciszewska, R A Baker, et al.

Extremophiles : Life Under Extreme Conditions|November 1, 2000

Cloning, expression, and characterization of pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralisM R Singleton, S J Taylor, J S Parrat, et al.

The EMBO Journal|March 15, 1996

The nature of inhibition of DNA gyrase by the coumarins and the cyclothialidines revealed by X-ray crystallographyR J Lewis, O M Singh, C V Smith, et al.

Journal of Molecular Biology|January 5, 1992

Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5 A resolutionD B Wigley, S J Gamblin, J P Turkenburg, et al.

Journal of Molecular Biology|August 5, 1994

Crystallization of inhibitor complexes of an N-terminal 24 kDa fragment of the DNA gyrase B proteinR J Lewis, O M Singh, C V Smith, et al.

Biochemical and Biophysical Research Communications|July 15, 1987

The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenaseK W Hart, A R Clarke, D B Wigley, et al.

Biochemistry|January 23, 1996

Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerasesH S Subramanya, D I Roper, Z Dauter, et al.

Journal of Molecular Biology|February 18, 1994

Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid filmsH Celia, L Hoermann, P Schultz, et al.

Biochimica Et Biophysica Acta|November 5, 1987

The engineering of a more thermally stable lactate dehydrogenase by reduction of the area of a water-accessible hydrophobic surfaceD B Wigley, A R Clarke, C R Dunn, et al.

Biochemical and Biophysical Research Communications|January 29, 1988

The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzymeA D Waldman, K W Hart, A R Clarke, et al.

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