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Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1.
The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems.
Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.
Crystal structures of two nitroreductases from hypervirulent Clostridium difficile and functionally related interactions with the antibiotic metronidazole.
Insights revealed by the co-crystal structure of the Saccharomyces cerevisiae histidine phosphotransfer protein Ypd1 and the receiver domain of its downstream response regulator Ssk1.
Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain.
Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1.
A common docking site for response regulators on the yeast phosphorelay protein YPD1.
Crystal structure and DNA binding activity of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291.
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin.
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.
Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae.
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.
Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane.
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.
Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.
Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB.
Crystallography X Ray