5E27
The structure of Resuscitation Promoting Factor B from M. tuberculosis reveals unexpected ubiquitin-like domains
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-12-20 |
Detector | MARRESEARCH |
Wavelength(s) | 0.94,0.97 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 102.376, 126.990, 86.286 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.600 |
R-factor | 0.22546 |
Rwork | 0.222 |
R-free | 0.29106 |
Structure solution method | MAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.827 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.600 |
Number of reflections | 17505 |
<I/σ(I)> | 31.5 |
Completeness [%] | 93.7 |
Redundancy | 16.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8.5 | 293 | 5 mg mL-1 protein, 18 % (v/v) ethanol in 50 mM sodium Tris-HCl buffer |