1HFD
HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1993-06 |
Detector | SIEMENS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.710, 51.150, 39.470 |
Unit cell angles | 90.00, 105.96, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.174 |
Rwork | 0.174 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1DSU MOLECULE B |
RMSD bond length | 0.012 |
RMSD bond angle | 28.580 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.083 | 0.242 |
Total number of observations | 36098 * | |
Number of reflections | 9267 | |
<I/σ(I)> | 15 | 2.8 |
Completeness [%] | 95.0 | 79 |
Redundancy | 4 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.4 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8-10 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | 0.1 (M) | ||
4 | 1 | reservoir | PEG6000 | 14-16 (%(w/v)) | |
5 | 1 | reservoir | MES | 50 (mM) | |
6 | 1 | reservoir | DMSO | 10 (%) |