3AB7
Crystal Structure of the Hypothetical Tandem-type Universal Stress Protein TTHA0350 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 | 2004-10-23 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.0 |
Spacegroup name | P 65 |
Unit cell lengths | 126.860, 126.860, 76.930 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.320 - 2.520 |
R-factor | 0.229 |
Rwork | 0.229 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.320 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 23907 | |
Completeness [%] | 97.5 | 77 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 500mM magnesium formate, 100mM HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |