2BGR
Crystal structure of HIV-1 Tat derived nonapeptides 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 | 2004-05-03 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 118.299, 127.043, 137.332 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.16 |
| Rwork | 0.160 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n1m |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.508 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.1999) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.070 | 0.370 |
| Number of reflections | 127470 | |
| <I/σ(I)> | 19.8 | 3.1 |
| Completeness [%] | 92.0 | 87.7 |
| Redundancy | 4.3 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
