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 |