2EG2
The crystal structure of PII protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-12-13 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 81.961, 81.961, 81.961 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.460 - 1.720 |
| R-factor | 0.194 |
| Rwork | 0.194 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2eg1 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.700 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 1.780 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.100 | 0.292 |
| Number of reflections | 9892 | |
| <I/σ(I)> | 29.7 | 8.77 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 14.7 | 14.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 291 | ammonium acetate, sodium acetate trihydrate, PEG4000, glycerol anhydrous, pH4.6, microbatch method, temperature 291K |
