2EGT
Crystal Structure of Hypothetical protein (AQ1549) from Aquifex aeolicus
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 | 2006-05-26 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97944 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 61.675, 61.675, 135.245 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.920 - 2.000 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2e8c |
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 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.066 | 0.422 |
Number of reflections | 10922 | |
Completeness [%] | 99.9 | 100 |
Redundancy | 19.7 | 20.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | 0.1M CHES, 40% MPD, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |