2WTL
Crystal structure of BfrA from M. tuberculosis
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] | 295 |
Detector technology | IMAGE PLATE |
Detector | MAR555 FLAT PANEL |
Spacegroup name | I 4 |
Unit cell lengths | 125.960, 125.960, 175.840 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.047 - 2.590 |
R-factor | 0.1849 |
Rwork | 0.183 |
R-free | 0.22830 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3bkn |
RMSD bond length | 0.016 |
RMSD bond angle | 2.090 |
Data reduction software | AUTOMAR |
Data scaling software | AUTOMAR |
Phasing software | PHENIX (AUTOMR WIZARD) |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.100 | 0.290 |
Number of reflections | 45901 | |
<I/σ(I)> | 6.7 | 1.6 |
Completeness [%] | 99.4 | 97.1 |
Redundancy | 4.4 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | PROTEIN (9MG/ML) WAS CRYSTALLIZED WITH 1.6M NACL; 100MM TRIS-HCL, PH 8.0 AT ROOM TEMPERATURE |