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 |