3GZD
Human selenocysteine lyase, P1 crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9800 |
| Spacegroup name | P 1 |
| Unit cell lengths | 66.640, 72.200, 89.430 |
| Unit cell angles | 83.91, 68.39, 86.96 |
Refinement procedure
| Resolution | 29.590 - 1.800 |
| R-factor | 0.1854 |
| Rwork | 0.184 |
| R-free | 0.21731 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gzc |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.455 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0035) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.051 | 0.527 |
| Number of reflections | 134466 | |
| <I/σ(I)> | 16.2 | 2.2 |
| Completeness [%] | 94.1 | 93.5 |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.1 | 293 | 50mM HEPES, 200mM Ammonium Nitrate, 25% PEG 3350, pH 8.1, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
