2EBG
Crystal structure of a hypothetical protein from thermus thermophilus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 180 |
| Detector technology | CCD |
| Collection date | 2006-03-14 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.798, 69.869, 73.673 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.690 - 1.800 |
| R-factor | 0.238 |
| Rwork | 0.238 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ebe |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.061 | 0.128 |
| Number of reflections | 21659 | |
| Completeness [%] | 97.2 | 80.8 |
| Redundancy | 11.4 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 25% PEG 3350, 0.1M Tris-cl, 0.2M MgCl2, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
