1ZZ1
Crystal structure of a HDAC-like protein with SAHA bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Wavelength(s) | 0.97848 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 68.606, 94.716, 123.924 |
Unit cell angles | 90.00, 104.75, 90.00 |
Refinement procedure
Resolution | 38.380 - 1.570 |
R-factor | 0.17366 |
Rwork | 0.172 |
R-free | 0.20132 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.456 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.630 |
High resolution limit [Å] | 1.570 | 1.570 |
Completeness [%] | 51.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | NaCl, Na-cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |