3CQ1
Structure of the DTDP-4-Keto-L-Rhamnose Reductase related protein (TT1362) from Thermus Thermophilus HB8
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-11-08 |
Detector | RIGAKU |
Wavelength(s) | 1.0 |
Spacegroup name | I 4 3 2 |
Unit cell lengths | 121.926, 121.926, 121.926 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.780 - 1.900 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.21900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cu6 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.070 | 0.344 |
Number of reflections | 12570 | |
Completeness [%] | 100.0 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | 0.1M Acetate, 12% PEG400, 0.1M Mg Chloride, pH4.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |