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 |