2CZ4
Crystal structure of a putative PII-like signaling protein (TTHA0516) from Thermus thermophilus HB8
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-12-11 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97889, 0.97939, 0.96000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 61.345, 117.699, 114.114 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.110 - 1.930 |
Rwork | 0.192 |
R-free | 0.22700 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.600 |
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] | 50.000 | 2.000 |
High resolution limit [Å] | 1.930 | 1.930 |
Number of reflections | 30273 | |
<I/σ(I)> | 18.9 | 4.9 |
Completeness [%] | 96.6 | 77.9 |
Redundancy | 7.7 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.1 | 293 | 0.1M Sodium acetate, 1.75M NaCl, pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K |