2DFA
Crystal Structure of Lactam Utilization Protein from Thermus thermophilus HB8
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 | CCD |
| Collection date | 2005-10-04 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.00 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 63.781, 63.826, 124.434 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.213 |
| Rwork | 0.213 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1v6t |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.300 |
| 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] | 30.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.058 | 0.435 |
| Number of reflections | 20371 | |
| <I/σ(I)> | 16.3 | 2.91 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 11.3 | 7.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6 | 295 | PEG600, PEG1000, MES, Glycerol, pH 6.0, microbatch, temperature 295K |
