2BMM
X-ray structure of a novel thermostable hemoglobin from the actinobacterium Thermobifida fusca
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 84.617, 84.617, 77.921 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 72.550 - 2.480 |
| R-factor | 0.223 |
| Rwork | 0.218 |
| R-free | 0.31500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ux8 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.551 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.470 |
| Rmerge | 0.050 |
| Number of reflections | 6119 |
| <I/σ(I)> | 17.3 |
| Completeness [%] | 96.7 |
| Redundancy | 8.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.8 | ACETATE BUFFER PH 5.8, NACL 2.5 M |
