PMID:10531496
| Citation |
MacPherson, KH, Carr, PD, Verger, D, Kwok, T, Davidson, BE and Ollis, DL (1999) Crystallization of the N-terminal domain of the Escherichia coli regulatory protein TyrR. Acta Crystallogr. D Biol. Crystallogr. 55:1923-4 |
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| Abstract |
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. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Crystallization; Dimerization; Escherichia coli; Escherichia coli Proteins; Peptide Fragments/chemistry; Recombinant Proteins/chemistry; Repressor Proteins/chemistry; X-Ray Diffraction |
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