2EHP
Crystal Structure of a Putative protein (AQ1627) from Aquifex aeolicus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2006-11-28 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97884, 0.9000, 0.97973 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 73.353, 53.873, 60.168 |
Unit cell angles | 90.00, 96.09, 90.00 |
Refinement procedure
Resolution | 19.970 - 1.300 |
R-factor | 0.227 |
Rwork | 0.227 |
R-free | 0.24000 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.350 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.034 | 0.204 |
Number of reflections | 51115 | |
Completeness [%] | 89.3 | 85.7 |
Redundancy | 6.7 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 293 | 40% Ethanol, 5% PEG1000, Phosphate-Citrate, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |