1WDE
Crystal structure of the conserved hypothetical protein APE0931 from Aeropyrum pernix K1
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 | 2004-04-16 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97909, 0.97940, 0.96400 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 62.827, 62.827, 129.728 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.530 - 2.000 |
R-factor | 0.199 |
Rwork | 0.199 |
R-free | 0.24400 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.700 |
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 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 18308 | |
<I/σ(I)> | 20.07 | 7.471 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.697 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 30% MPD, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |