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T C Terwilliger

Showing results (11-20 of 68) with videos related to

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Acta Crystallographica. Section D, Biological Crystallography|October 26, 1999
Reciprocal-space solvent flatteningT C Terwilliger
Acta Crystallographica. Section D, Biological Crystallography|January 1, 1994
MAD phasing: Bayesian estimates of F(A)T C Terwilliger
Acta Crystallographica. Section D, Biological Crystallography|May 18, 1999
Sigma2R, a reciprocal-space measure of the quality of macromolecular electron-density mapsT C Terwilliger
The Journal of Biological Chemistry|June 10, 1982
The structure of melittin. II. Interpretation of the structureT C Terwilliger, D Eisenberg
Genetica|March 11, 2000
Exploring structure space. A protein structure initiativeT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|March 25, 1999
Automated MAD and MIR structure solutionT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|March 25, 1999
Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methodsT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|July 1, 1996
Bayesian weighting for macromolecular crystallographic refinementT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|October 26, 1999
Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. densityT C Terwilliger, J Berendzen
The Journal of Biological Chemistry|June 10, 1982
The structure of melittin. I. Structure determination and partial refinementT C Terwilliger, D Eisenberg
Pageof 7

Showing results (11-20 of 68) with videos related to

Sort By:
Pageof 7
Acta Crystallographica. Section D, Biological Crystallography|October 26, 1999
Reciprocal-space solvent flatteningT C Terwilliger
Acta Crystallographica. Section D, Biological Crystallography|January 1, 1994
MAD phasing: Bayesian estimates of F(A)T C Terwilliger
Acta Crystallographica. Section D, Biological Crystallography|May 18, 1999
Sigma2R, a reciprocal-space measure of the quality of macromolecular electron-density mapsT C Terwilliger
The Journal of Biological Chemistry|June 10, 1982
The structure of melittin. II. Interpretation of the structureT C Terwilliger, D Eisenberg
Genetica|March 11, 2000
Exploring structure space. A protein structure initiativeT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|March 25, 1999
Automated MAD and MIR structure solutionT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|March 25, 1999
Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methodsT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|July 1, 1996
Bayesian weighting for macromolecular crystallographic refinementT C Terwilliger, J Berendzen
Acta Crystallographica. Section D, Biological Crystallography|October 26, 1999
Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. densityT C Terwilliger, J Berendzen
The Journal of Biological Chemistry|June 10, 1982
The structure of melittin. I. Structure determination and partial refinementT C Terwilliger, D Eisenberg
Pageof 7