1VGG
Crystal Structure of the Conserved Hypothetical Protein TTHA1091 from Thermus Thermophilus HB8
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-02-03 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9722, 0.9794, 0.9798 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 85.490, 100.440, 104.690 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.930 - 1.750 |
| R-factor | 0.182 |
| Rwork | 0.180 |
| R-free | 0.20400 |
| Structure solution method | MAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.057 | 0.134 |
| Number of reflections | 90161 | |
| <I/σ(I)> | 27.9 | 9.8 |
| Completeness [%] | 99.0 | 100 |
| Redundancy | 5.3 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | PEG 200, sodium acetate, sodium chloride, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |
