1LKT
CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 300 |
Detector technology | IMAGE PLATE |
Collection date | 1996-04 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 57.300, 82.100, 73.800 |
Unit cell angles | 90.00, 90.90, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.600 |
R-factor | 0.186 * |
Rwork | 0.199 |
Structure solution method | MIR |
RMSD bond length | 0.009 * |
RMSD bond angle | 1.490 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.650 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.076 | 0.298 |
Total number of observations | 48766 * | |
Number of reflections | 20822 | |
Completeness [%] | 96.5 | 72.2 |
Redundancy | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.6 | 20% PEG 8K, 0.2 M MGCL2, 0.1 M BIS-TRIS, PH 6.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 20 (%(w/v)) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | Bis-Tris-HCl | 0.1 (M) |