1XJE
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dTTP-GDP complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-08-23 |
Detector | MARRESEARCH |
Wavelength(s) | 0.811 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 119.391, 124.376, 107.243 |
Unit cell angles | 90.00, 103.68, 90.00 |
Refinement procedure
Resolution | 18.000 - 1.900 |
R-factor | 0.18445 |
Rwork | 0.182 |
R-free | 0.22268 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1r1r |
RMSD bond length | 0.019 |
RMSD bond angle | 1.780 |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 119507 | |
<I/σ(I)> | 12.23 | 3.2 |
Completeness [%] | 97.2 | 96.6 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | PEG8000, sodium acetate, sodium chloride, dithiotreithol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |