1BIO
HUMAN COMPLEMENT FACTOR D IN COMPLEX WITH ISATOIC ANHYDRIDE INHIBITOR
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.480, 49.910, 39.430 |
Unit cell angles | 90.00, 105.69, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.186 |
Rwork | 0.186 |
R-free | 0.19100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1DSU MOLECULE B |
RMSD bond length | 0.009 |
RMSD bond angle | 27.570 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.051 | 0.253 |
Total number of observations | 133846 * | |
Number of reflections | 31552 | |
<I/σ(I)> | 29 | 5.5 |
Completeness [%] | 95.0 | 90 |
Redundancy | 4.1 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.4 | 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 | drop | DMSO-dissolved IA | a molar ratio of 20:1 | |
5 | 1 | reservoir | PEG6000 | 14-16 (%(w/v)) | |
6 | 1 | reservoir | MES | 50 (mM) | |
7 | 1 | reservoir | DMSO | 10 (%) |