2RBF
Structure of the ribbon-helix-helix domain of Escherichia coli PutA (PutA52) complexed with operator DNA (O2)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-08-06 |
| Detector | NOIR-1 |
| Wavelength(s) | 1.24 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.911, 44.084, 55.230 |
| Unit cell angles | 90.00, 101.50, 90.00 |
Refinement procedure
| Resolution | 54.150 - 2.250 |
| R-factor | 0.208 |
| Rwork | 0.206 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ay0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.591 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 54.153 | 44.540 | 2.370 |
| High resolution limit [Å] | 2.250 | 7.120 | 2.250 |
| Rmerge | 0.059 | 0.036 | 0.434 |
| Total number of observations | 1103 | 5336 | |
| Number of reflections | 10293 | ||
| <I/σ(I)> | 8.2 | 16.2 | 1.6 |
| Completeness [%] | 99.5 | 95.3 | 99.3 |
| Redundancy | 3.6 | 3.3 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 30% PEG-MME 550, 50 mM CaCl2, and 100 mM Bis-Tris pH 6.5., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | PEG-MME 550 | ||
| 2 | 1 | 1 | CaCl2 | ||
| 3 | 1 | 1 | Bis-Tris | ||
| 4 | 1 | 2 | PEG-MME 550 | ||
| 5 | 1 | 2 | CaCl2 | ||
| 6 | 1 | 2 | Bis-Tris |
