2BGN
HIV-1 Tat protein derived N-terminal nonapeptide Trp2-Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-02-07 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 158.945, 170.273, 239.200 |
| Unit cell angles | 90.00, 100.93, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.150 |
| R-factor | 0.227 |
| Rwork | 0.227 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w1i |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.518 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.260 |
| High resolution limit [Å] | 3.150 | 3.150 |
| Rmerge | 0.110 | 0.410 |
| Number of reflections | 97782 | |
| <I/σ(I)> | 9.7 | 2.6 |
| Completeness [%] | 89.0 | 81 |
| Redundancy | 2.5 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
