Crystallization of the N-terminal domain of the Escherichia coli regulatory protein TyrR.
The N-terminal domain of the regulatory protein TyrR from Escherichia coli forms a dimer in solution and has been purified and crystallized. The crystals belong to space group C2 with unit-cell parameters a = 134.5, b = 72.1, c = 96.7 A, beta = 98.5 degrees. The crystals diffract to 2.8 A. Assuming a molecular weight of 23219 Da, a V(m) of 2.5 A(3) Da(-1) is obtained for two dimers in the asymmetric unit.
MacPherson
K H
KH
Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.
Carr
P D
PD
Verger
D
D
Kwok
T
T
Davidson
B E
BE
Ollis
D L
DL
D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D019281:Dimerization; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D012097:Repressor Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012097:Repressor Proteins; C069256:TyrR protein, E coli