1FDP
PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 95 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-02-01 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.050, 70.320, 86.300 |
| Unit cell angles | 90.00, 101.98, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.204 |
| Rwork | 0.204 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | CORE REGION OF FACTOR D (1DSU MOLECULE B) |
| RMSD bond length | 0.008 |
| RMSD bond angle | 28.410 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.066 | 0.234 |
| Total number of observations | 93825 * | |
| Number of reflections | 43713 | |
| <I/σ(I)> | 13.8 | 3.9 |
| Completeness [%] | 98.5 | 96.8 |
| Redundancy | 2.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7 * | 298 | CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000 AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 0.1 (M) | ||
| 4 | 1 | reservoir | PEG6000 | 10-12 (%) | |
| 5 | 1 | reservoir | MES | 30 (mM) |
