1RFE
Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-06-26 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.979 |
Spacegroup name | P 43 2 2 |
Unit cell lengths | 49.309, 49.309, 132.588 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.390 - 2.000 |
R-factor | 0.20572 |
Rwork | 0.202 |
R-free | 0.28106 |
Structure solution method | SAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.689 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.390 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.177 | 0.790 |
Number of reflections | 127155 | |
<I/σ(I)> | 11.68 | 1.23 |
Completeness [%] | 98.8 | 76.7 |
Redundancy | 10.87 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 290 | 25% PEG 4000 , pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 290K |