5AWE
Crystal structure of a hypothetical protein, TTHA0829 from Thermus thermophilus HB8, composed of cystathionine-beta-synthase (CBS) and aspartate-kinase chorismate-mutase tyrA (ACT) domains
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 | CCD |
| Collection date | 2004-06-25 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 0.97911 |
| Spacegroup name | P 62 2 2 |
| Unit cell lengths | 90.800, 90.800, 89.750 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 40.510 - 2.450 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.26100 |
| Structure solution method | SAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.100 |
| Data scaling software | HKL-2000 |
| Phasing software | SnB |
| Refinement software | CNS (1.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.510 | 2.540 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.104 | 0.305 |
| Number of reflections | 8426 | |
| <I/σ(I)> | 31.7 | 4.6 |
| Completeness [%] | 99.6 | 98.2 |
| Redundancy | 16.4 | 14.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | HEPES, magnesium chloride, PEG 400 |
