2EIU
Crystal Structure of a Putative protein (AQ1627) 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 | 2006-11-28 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 75.022, 174.092, 58.112 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.800 - 2.000 |
R-factor | 0.23 |
Rwork | 0.230 |
R-free | 0.25700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ehp |
RMSD bond length | 0.009 |
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] | 40.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.079 | 0.335 |
Number of reflections | 50865 | |
Completeness [%] | 97.8 | 99.5 |
Redundancy | 7.4 | 8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 20% PEG 3350, 0.2M Magnesium acetate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |