2I76
Crystal structure of protein TM1727 from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-06-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | H 3 |
| Unit cell lengths | 130.276, 130.276, 97.612 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.840 - 3.000 |
| R-factor | 0.236 |
| Rwork | 0.236 |
| R-free | 0.28800 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.500 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHARP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.106 | 0.710 |
| Number of reflections | 37927 | |
| <I/σ(I)> | 9.4 | |
| Completeness [%] | 99.9 | 99.5 |
| Redundancy | 5.6 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 30% PEG 3350, 0.25M Ammonium Acetate, 0.1M Bis-Tris, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
