1AA0
FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1995-07-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | H 3 2 |
Unit cell lengths | 41.200, 41.200, 358.700 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.200 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.26700 * |
Structure solution method | MIR |
RMSD bond length | 0.010 * |
RMSD bond angle | 1.300 * |
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] | 30.000 | 2.240 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.053 * | |
Total number of observations | 57901 * | |
Number of reflections | 6490 * | |
<I/σ(I)> | 15 | 2 |
Completeness [%] | 92.6 | 56.6 |
Redundancy | 4.8 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 22 * | PROTEIN WAS CRYSTALLIZED AT 22OC USING 34% PEG400, 0.1M ZN ACETATE IN 0.1M MES BUFFER AT PH6.0 AS WELL SOLUTION BY MIXING EQUAL AMOUNT OF WELL SOLUTION AND PROTEIN SOLUTION AT 29MG/ML IN A HANGING DROP, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 29 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | pH7.5 |
3 | 1 | reservoir | PEG400 | 34 (%) | |
4 | 1 | reservoir | zinc acetate | 0.1 (M) | |
5 | 1 | reservoir | MES | 0.1 (M) | pH6.0 |