1J27
Crystal structure of a hypothetical protein, TT1725, from Thermus thermophilus HB8 at 1.7A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 62.533, 68.388, 58.851 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.480 - 1.700 |
R-factor | 0.178 |
Rwork | 0.178 |
R-free | 0.21800 |
Structure solution method | MAD |
RMSD bond length | 0.020 |
RMSD bond angle | 24.300 * |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 1.700 | 1.700 * |
Rmerge | 0.028 * | 0.097 * |
Total number of observations | 71421 * | |
Number of reflections | 15362 | |
Completeness [%] | 98.7 * | 89.6 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 * | 20 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 1.9 (mg/ml) | |
2 | 1 | drop | Tris | 10 (mM) | pH8.5 |
3 | 1 | drop | PEG3350 | 2.5 (%) | |
4 | 1 | drop | sodium sulfate | 75 (mM) |