1VGG
Crystal Structure of the Conserved Hypothetical Protein TTHA1091 from Thermus Thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-02-03 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9722, 0.9794, 0.9798 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 85.490, 100.440, 104.690 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.930 - 1.750 |
R-factor | 0.182 |
Rwork | 0.180 |
R-free | 0.20400 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.057 | 0.134 |
Number of reflections | 90161 | |
<I/σ(I)> | 27.9 | 9.8 |
Completeness [%] | 99.0 | 100 |
Redundancy | 5.3 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | PEG 200, sodium acetate, sodium chloride, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K |