4B1A
Crystal structure of lysozyme with Keggin molecule
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 160 |
Detector technology | CCD |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 77.960, 77.960, 36.410 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.380 - 1.670 |
R-factor | 0.21501 |
Rwork | 0.212 |
R-free | 0.26664 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 193l |
RMSD bond length | 0.022 |
RMSD bond angle | 1.840 |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.380 | 1.760 |
High resolution limit [Å] | 1.670 | 1.670 |
Rmerge | 0.020 | 0.100 |
Number of reflections | 13544 | |
<I/σ(I)> | 29.7 | 6.4 |
Completeness [%] | 99.6 | 100 |
Redundancy | 13.5 | 13.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.5 | 2-10% (M/V) NACL AND 0.1 M ACETATE BUFFER PH 4.5 (THE PROTEIN:WELL SOLUTION RATIO IN THE DROP WAS 1:1 WITH THE FINAL DROP VOLUME OF 4 MICROLITER USING A PROTEIN STOCK CONCENTRATION OF AROUND 50 MG/ML. |