3B5M
Crystal structure of conserved uncharacterized protein from Rhodopirellula baltica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2006-10-05 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97958 |
| Spacegroup name | P 1 |
| Unit cell lengths | 49.268, 58.315, 73.799 |
| Unit cell angles | 93.89, 91.12, 90.10 |
Refinement procedure
| Resolution | 20.000 - 1.210 |
| R-factor | 0.17713 |
| Rwork | 0.176 |
| R-free | 0.20237 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2nr4 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.439 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.3.0034) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.250 |
| High resolution limit [Å] | 1.210 | 1.210 |
| Rmerge | 0.063 | 0.580 |
| Number of reflections | 231519 | |
| <I/σ(I)> | 6.6 | 1.3 |
| Completeness [%] | 92.7 | 79.5 |
| Redundancy | 3.8 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.5 | 294 | 100mM Bis-tris pH 5.5, 25% PEG 3350, 200mM Ammonium sulfate, VAPOR DIFFUSION, temperature 294K |
