6GPC
Crystal structure of the arginine-bound form of domain 1 from TmArgBP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-11-11 |
| Detector | RIGAKU SATURN 944 |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 1 |
| Unit cell lengths | 35.530, 45.932, 52.510 |
| Unit cell angles | 115.91, 109.53, 90.02 |
Refinement procedure
| Resolution | 14.620 - 1.750 |
| R-factor | 0.1644 |
| Rwork | 0.162 |
| R-free | 0.20174 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4prs |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.044 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.620 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.062 | |
| Number of reflections | 25022 | |
| <I/σ(I)> | 22.1 | |
| Completeness [%] | 89.4 | |
| Redundancy | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | The best crystals of D1 domain were obtained using a protein concentration of 8 mg/ml in a solution containing 0.2 M NaCl, 0.1M Bis-Tris (pH 5.5), 25% (w/v) polyethylene glycol (PEG) 3,350. |
