1C5E
BACTERIOPHAGE LAMBDA HEAD PROTEIN D
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-04-01 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.580, 69.070, 45.590 |
Unit cell angles | 90.00, 104.32, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.100 |
R-factor | 0.0982 * |
R-free | 0.13280 |
Structure solution method | MAD |
RMSD bond length | 0.014 |
RMSD bond angle | 0.031 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SHELXL-97 |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.120 |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.046 * | |
Total number of observations | 635194 * | |
Number of reflections | 109996 | |
Completeness [%] | 99.2 | 98.3 |
Redundancy | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 28% PEG 4000, 0.1 M BIS-TRIS PH 6.5, 10 % GLYCEROL |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris | 20 (mM) | |
3 | 1 | reservoir | PEG4000 | 28 (%) | |
4 | 1 | reservoir | Bis-Tris | 0.1 (M) | |
5 | 1 | reservoir | glycerol | 10 (%) |