5OBG
Crystal structure of glycine binding protein in complex with strychnine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 150 |
| Detector technology | CCD |
| Collection date | 2017-04-11 |
| Detector | RIGAKU SATURN 944+ |
| Wavelength(s) | 1.54157 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 90.353, 100.040, 163.752 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.920 - 2.000 |
| R-factor | 0.19928 |
| Rwork | 0.197 |
| R-free | 0.24961 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5oan |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.950 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.920 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.147 | 0.589 |
| Number of reflections | 100843 | 4919 |
| <I/σ(I)> | 6.1 | 1.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.2 | 6.2 |
| CC(1/2) | 0.992 | 0.657 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Reservoir buffer: 20 % PEG 3350, 0.2 M MgOAc Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 0.5 mM strychnine |






