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Expression, Purification, Crystallization and Molecular Replacement Studies of TorI, an Inhibition Protein of Tor System
Authors:HUANG Wei  YUAN Cai  Ansaldi Mireille  Morelli Xavier  Edward J. Meehan  CHEN Li-Qing  HUANG Ming-Dong
Abstract:TorI, a Tor system inhibitor acting through protein-protein interaction with the TorR response regulator, is an excisionase that interacts with the integrase and DNA during prophage excision. It has been crystallized by the vapor-diffusion method using polyethylene glycol 3350 as a precipitant at pH 8.5. The X-ray diffraction data sets from the TorI crystal was collected at a resolution of 2.1 (A), using a synchrotron source. The crystal belongs to primitive monoclinic lattice with cell parameters of 46.210(A) × 53.992(A) × 73.561(A)
Keywords:TorI  inhibitor  crystallization  X-ray diffraction  Expression  Purification  Studies  Replacement  Molecular  Crystallization  System  Protein  primitive  lattice  cell parameters  synchrotron  source  diffraction  data  sets  crystal  resolution  method  polyethylene glycol
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