2VCG
Crystal structure of a HDAC-like protein HDAH from Bordetella sp. with the bound inhibitor ST-17
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-03-28 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.664, 93.633, 121.664 |
| Unit cell angles | 90.00, 103.99, 90.00 |
Refinement procedure
| Resolution | 117.850 - 1.900 |
| R-factor | 0.159 |
| Rwork | 0.156 |
| R-free | 0.20600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1zz0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.345 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.360 |
| Number of reflections | 111630 | |
| <I/σ(I)> | 16.9 | 4.2 |
| Completeness [%] | 96.0 | 93.8 |
| Redundancy | 2.9 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 600 MM NACL 200 MM NA-CACODYLATE 6.5 |
