1EE8
CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.421, 61.289, 98.342 |
| Unit cell angles | 90.00, 91.71, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.214 * |
| Rwork | 0.214 |
| R-free | 0.25800 |
| RMSD bond length | 0.006 * |
| RMSD bond angle | 1.350 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.070 * | 0.620 * |
| Total number of observations | 402397 * | |
| Number of reflections | 37892 | 1729 * |
| <I/σ(I)> | 29.1 | |
| Completeness [%] | 90.0 * | 82.1 * |
| Redundancy | 4.4 | 3.96 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 9.8 | 293 | Sugahara, M., (2000) J. Biochem., 127, 9. * |
