1HZ5
CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS, WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-05-10 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 66.437, 66.437, 109.181 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 24.660 - 1.800 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.19300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CRYSTAL STRUCTURE OF B1 DOMAIN (Y47W) NON -HIS-TAG COORDINATE STRUCTURE (SEE 1HZ6) |
| RMSD bond length | 0.006 |
| RMSD bond angle | 26.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.066 | 0.280 |
| Number of reflections | 26449 | |
| <I/σ(I)> | 18.5 | 3.7 |
| Completeness [%] | 99.8 | 98 |
| Redundancy | 4.4 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 0.2M Zinc Accetate and MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | 150 (mM) | ||
| 2 | 1 | reservoir | PEG8000 | 1 (%) | |
| 3 | 1 | reservoir | MES | 50 (mM) | |
| 4 | 1 | reservoir | glycerol | 25 (%) | cryoprotectant |
| 5 | 1 | reservoir | PEG400 | 5 (%) | cryoprotectant |
