2Z9N
Crystal structure of cameline peptidoglycan recognition protein at 3.2 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-06-15 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 89.855, 102.456, 164.043 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.200 |
| Rwork | 0.215 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2r2k |
| RMSD bond length | 0.010 |
| RMSD bond angle | 2.000 |
| Data reduction software | DENZO |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Number of reflections | 12274 | |
| <I/σ(I)> | 6.9 | 11 |
| Completeness [%] | 88.7 | 92.2 |
| Redundancy | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 25% PEG 3350, 2M Sodium tartrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
