2EGR
Crystal Structure of Hypothetical Protein(AQ1494) from Aquifex aeolicus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B2 |
| Temperature [K] | 180 |
| Detector technology | CCD |
| Collection date | 2006-12-17 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 64 |
| Unit cell lengths | 102.482, 102.482, 53.067 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.550 - 1.800 |
| R-factor | 0.22121 |
| Rwork | 0.220 |
| R-free | 0.24455 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2egi |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.535 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.058 | 0.373 |
| Number of reflections | 29594 | |
| Completeness [%] | 99.7 | 99.8 |
| Redundancy | 10.6 | 10.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | oil batch | 8.5 | 293 | 0.1M Tris-HCl pH8.5, 2M Ammonium Sulfate, 15% Glycerol, oil batch, temperature 293K |
