2ODQ
Complement component C2a, the catalytic fragment of C3- and C5-convertase of human complement
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-03-20 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.354, 84.201, 74.426 |
Unit cell angles | 90.00, 92.10, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.300 |
R-factor | 0.217 |
Rwork | 0.214 |
R-free | 0.27400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rrk |
RMSD bond length | 0.027 |
RMSD bond angle | 2.313 |
Data reduction software | d*TREK |
Data scaling software | d*TREK |
Phasing software | CNS |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.047 | 0.180 |
Number of reflections | 27904 | |
<I/σ(I)> | 19.5 | 7.1 |
Completeness [%] | 98.8 | 97.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | 20% PEG 10000, 0.1M HEPES, 0.3M glycyl-glycyl-glycine, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |