1AVY
FIBRITIN DELETION MUTANT M (BACTERIOPHAGE T4)
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-09-01 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 3 |
Unit cell lengths | 43.680, 43.680, 90.610 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 23.000 - 1.850 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.25300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aa0 |
RMSD bond length | 0.006 |
RMSD bond angle | 24.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.000 | 1.910 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.036 * | 0.182 * |
Total number of observations | 39783 * | |
Number of reflections | 14861 | |
Completeness [%] | 89.8 | 53.6 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | HANGING DROPS WITH 20MG/ML PROTEIN AND 1.75M LI2SO4, 0.1M TRIS-HCL, PH7.5, AS PRECIPITANT, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Na phosphate | 5 (mM) | |
3 | 1 | drop | 0.875 (M) | ||
4 | 1 | drop | Tris-HCl | 0.05 (M) | |
5 | 1 | reservoir | 1.75 (M) | ||
6 | 1 | reservoir | Tris-HCl | 0.1 (M) |