2E55
Structure of AQ2163 protein from Aquifex aeolicus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-10-04 |
| Detector | RIGAKU |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.390, 70.670, 90.166 |
| Unit cell angles | 90.00, 97.96, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.150 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1v9s |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.290 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.082 | 0.276 |
| Number of reflections | 37617 | |
| <I/σ(I)> | 7.7 | 3.1 |
| Completeness [%] | 99.0 | 95 |
| Redundancy | 3.8 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.6 | 295 | 32% PEG 4K, 0.1M LiSO4, 0.13M Tris-hydrochloride, pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
