1WDV
Crystal structure of hypothetical protein APE2540
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 | 2003-11-27 |
Detector | RIGAKU JUPITER |
Wavelength(s) | 0.964, 0.9792, 0.9796 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 47.435, 58.917, 53.603 |
Unit cell angles | 90.00, 106.80, 90.00 |
Refinement procedure
Resolution | 29.980 - 1.700 |
R-factor | 0.169 |
Rwork | 0.169 |
R-free | 0.20600 |
Structure solution method | MAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.500 |
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 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 31231 | |
<I/σ(I)> | 20.9 | 13.5 |
Completeness [%] | 99.9 | 100 |
Redundancy | 5.29 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.6 | 293 | 16.5% PEG20000, 0.1M HEPES pH 7.6, micro batch, temperature 293K |