3C10
Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)
Replaces: 2PQPExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-20 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.10000 |
| Spacegroup name | P 32 |
| Unit cell lengths | 81.827, 81.827, 148.970 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.420 - 2.000 |
| R-factor | 0.20428 |
| Rwork | 0.201 |
| R-free | 0.26312 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2NVR |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.689 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.041 | 0.238 |
| Number of reflections | 73439 | |
| <I/σ(I)> | 26.3 | 3.6 |
| Completeness [%] | 97.5 | 79 |
| Redundancy | 3.1 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 300 | 20 % PEG 3350, 0.1 M HEPES pH 7.5, 10 % Isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 300K |
