2BFV
MONOCLONAL ANTIBODY FRAGMENT FV4155 FROM E. COLI
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1995-04 |
Detector | RIGAKU |
Spacegroup name | P 32 |
Unit cell lengths | 53.600, 53.600, 83.800 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.500 |
R-factor | 0.176 * |
Rwork | 0.187 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nbv |
RMSD bond length | 0.011 |
RMSD bond angle | 0.037 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((ROTAVATA)) |
Phasing software | AMoRE |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.064 * | 0.225 * |
Total number of observations | 12233 * | |
Number of reflections | 7836 | |
<I/σ(I)> | 7.21 | 2.6 |
Completeness [%] | 86.9 | 87.5 |
Redundancy | 1.5 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 15% (W/V) PEG 4000, 100MM NA ACETATE AND 50MM TRIS HCL PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2.5-3 (mg/ml) | |
2 | 1 | drop | Na acetate | 0.05 (M) | |
3 | 1 | drop | Tris-HCl | 0.025 (M) | |
4 | 1 | drop | PEG4000 | 7.5 (%(w/v)) | |
5 | 1 | reservoir | Na acetate | 0.1 (M) | |
6 | 1 | reservoir | Tris-HCl | 0.05 (M) | |
7 | 1 | reservoir | PEG4000 | 15 (%(w/v)) |