2EI5
Crystal Structure of Hypothetical protein(TTHA0061) from Thermus thermophilus
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 | CCD |
Collection date | 2005-09-30 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 65 |
Unit cell lengths | 48.094, 48.094, 150.631 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.650 - 1.880 |
R-factor | 0.201 |
Rwork | 0.201 |
R-free | 0.24100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ebg |
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] | 50.000 | 1.950 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.038 | 0.239 |
Number of reflections | 15964 | |
Completeness [%] | 99.8 | 98.9 |
Redundancy | 10.2 | 7.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 28% PEG MME2000, 0.1M Bis-Tris pH6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |