1LPI
HEW LYSOZYME: TRP...NA CATION-PI INTERACTION
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Temperature [K] | 278 |
Detector technology | IMAGE PLATE |
Collection date | 1995-09 |
Detector | MARRESEARCH |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 79.100, 79.100, 37.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.000 - 2.000 |
R-factor | 0.17 * |
R-free | 0.24000 * |
Starting model (for MR) | 1hel |
RMSD bond length | 0.005 |
RMSD bond angle | 0.020 |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | SHELXL-96 |
Refinement software | SHELXL-96 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 3.000 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.096 * | 0.188 * |
Number of reflections | 7717 | |
<I/σ(I)> | 14.08 | 10.01 |
Completeness [%] | 98.5 | 99.09 |
Redundancy | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 4.6 | PROTEIN WAS CRYSTALLIZED FROM 2% NANO3, IN A 100 MM SODIUM ACETATE BUFFER, PH 4.6; THE PROTEIN STOCK SOLUTION CONTAINED 20 MG/ML |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 1 | 2 (%) | ||
3 | 1 | 1 | sodium acetate | 0.1 (M) |