2GJM
Crystal structure of Buffalo lactoperoxidase at 2.75A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-03-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.240, 80.472, 77.348 |
| Unit cell angles | 90.00, 102.71, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.750 |
| R-factor | 0.182 |
| Rwork | 0.182 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mhl |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.500 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.790 |
| High resolution limit [Å] | 2.750 | 2.750 |
| Number of reflections | 16282 | |
| <I/σ(I)> | 8.5 | 2.1 |
| Completeness [%] | 96.0 | 95.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 290 | TRIS-HCL, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
