1GPO
CRYSTAL STRUCTURE OF THE RATIONALLY DESIGNED ANTIBODY M41 AS A FAB FRAGMENT
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-03 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 96.470, 103.510, 113.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.950 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.28300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | HYBRID FAB FRAGMENT CONSISTING OF THE MODELLED STRUCTURE FOR THE ARTIFICIAL FV FRAGMENT M41 AND CONSTANT DOMAINS OF THE ANTI-LYSOZYME ANTIBODY HYHEL-10 |
RMSD bond length | 0.011 |
RMSD bond angle | 28.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.000 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.065 | 0.215 |
Number of reflections | 69136 | |
Completeness [%] | 84.6 | 50.2 |
Redundancy | 2.6 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 | 18 * | Schiweck, W., (1995) Proteins: Struct.,Funct., Genet., 23, 561. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulphate | 2.0 (M) | |
2 | 1 | reservoir | DMSO | 5 (%(v/v)) | |
3 | 1 | reservoir | sodium cacodylate | 100 (mM) |