1DSF
THE CRYSTAL STRUCTURE OF THE DISULFIDE-STABILIZED FV FRAGMENT OF ANTICANCER ANTIBODY B1: CONFORMATIONAL INFLUENCE OF AN ENGINEERED DISULFIDE BOND
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1995-12 |
Detector | SIEMENS |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 80.100, 80.100, 138.200 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.000 |
R-factor | 0.182 |
Rwork | 0.182 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1IGG |
RMSD bond length | 0.014 |
RMSD bond angle | 2.740 |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.800 | 2.200 |
High resolution limit [Å] | 2.120 | 2.120 |
Rmerge | 0.066 * | |
Number of reflections | 14289 | |
<I/σ(I)> | 6.8 | 1.5 |
Completeness [%] | 92.0 | 58 |
Redundancy | 6 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 1.6M HEPES PH-7.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | HEPES-HCl | 10 (mM) | |
3 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
4 | 1 | reservoir | HEPES | 0.1 (M) |