2F4I
Crystal structure of an ob-fold protein (tm0957) from thermotoga maritima msb8 at 1.90 A resolution
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-04 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97942, 0.95372 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.677, 78.075, 82.487 |
| Unit cell angles | 90.00, 93.40, 90.00 |
Refinement procedure
| Resolution | 29.830 - 2.250 |
| R-factor | 0.19279 |
| Rwork | 0.190 |
| R-free | 0.24800 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.562 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.830 | 2.370 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.090 | 0.300 |
| Number of reflections | 39599 | |
| <I/σ(I)> | 5.8 | 2.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 277 | 0.2M MgCl2, 30.0% PEG-4000, 0.1M TRIS, pH 8.5, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |
