1V9A
Crystal structure of Uroporphyrin-III C-methyl transferase from Thermus thermophilus complexed with S-adenyl homocysteine
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 | IMAGE PLATE |
| Collection date | 2003-12-08 |
| Detector | RIGAKU RAXIS |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 59.982, 63.810, 132.422 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.500 - 2.000 |
| R-factor | 0.215 |
| Rwork | 0.215 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cbf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.600 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.500 | 2.000 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.072 | 0.486 |
| Number of reflections | 38702 | |
| <I/σ(I)> | 15.1 | 3.03 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.97 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.3 | 291 | Citrate, PEG 20000, pH 5.3, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
