2OU2
Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-20 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 107.632, 107.632, 133.731 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 83.920 - 2.300 |
| R-factor | 0.22145 |
| Rwork | 0.220 |
| R-free | 0.25215 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2giv |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.455 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 83.920 |
| High resolution limit [Å] | 2.300 |
| Rmerge | 0.059 |
| Number of reflections | 17598 |
| <I/σ(I)> | 9.2 |
| Completeness [%] | 98.8 |
| Redundancy | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 293 | Purified HTATIP was complexed with acetylcoenzyme A (AcCoA) (Sigma) at 1:10 molar ratio of protein:AcCoA and crystallized using the hanging drop vapor diffusion method at 20 deg C by mixing 1 microliter of the protein solution with 1 microliter of the reservoir solution containing 16% PEG3350, 0.2 M ammonium acetate, 0.1 M Bis-Tris, pH 6.6., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
