1WYT
Crystal structure of glycine decarboxylase (P-protein) of the glycine cleavage system, in apo form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 90 |
| Detector technology | IMAGE PLATE |
| Collection date | 2002-03-05 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 89.554, 89.554, 371.052 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.350 - 2.400 |
| R-factor | 0.18 |
| Rwork | 0.177 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | P-PROTEIN IN THE HOLO-FORM |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.148 | 0.473 |
| Number of reflections | 69153 | |
| <I/σ(I)> | 15.3 | 5.2 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 10.2 | 9.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | PEG 3350, KSCN, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
