1W74
X-ray structure of peptidyl-prolyl cis-trans isomerase A, PpiA, Rv0009, from Mycobacterium tuberculosis.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2004-02-01 |
| Detector | ADSC CCD |
| Spacegroup name | P 31 |
| Unit cell lengths | 65.349, 65.349, 102.493 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.600 |
| R-factor | 0.213 |
| Rwork | 0.212 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1awr |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.404 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.620 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.100 | 0.590 |
| Number of reflections | 14896 | |
| <I/σ(I)> | 6.2 | 1.3 |
| Completeness [%] | 99.6 | 99.8 |
| Redundancy | 5.4 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | PROTEIN WAS CO-CRYSTALLIZED WITH THE PEPTIDE HAGPIA (FINAL CONCENTRATION 1 MM) FROM 30% PEG-200, 5% PEG-3000, 0.1 M MES-HCL PH 6.0; THEN SOAKED IN THE RESERVOIR SOLUTION PLUS 1 MM HAGPIA. |
