2E85
Crystal Structure of the Hydrogenase 3 Maturation protease
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 | 2006-04-18 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97921, 0.97955, 1.0000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 87.425, 54.984, 67.964 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.700 |
R-factor | 0.248 |
Rwork | 0.248 |
R-free | 0.25800 |
Structure solution method | MAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
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 |
Rmerge | 0.084 | 0.231 |
Number of reflections | 36372 | |
<I/σ(I)> | 19.54 | 5.84 |
Completeness [%] | 98.6 | 97.7 |
Redundancy | 6.5 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.2M CaCl2, 0.1M Sodium Hepes, 28% PEG 400, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |