2BSD
Structure of Lactococcal Bacteriophage p2 Receptor Binding Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.108, 96.250, 149.491 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.221 |
Rwork | 0.220 |
R-free | 0.25200 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.148 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE/RESOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.090 | 0.330 |
Number of reflections | 48171 | |
<I/σ(I)> | 6.7 | 2 |
Completeness [%] | 99.0 | |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | A VOLUME OF 1 MICROL OF PROTEIN 6 TO 9 MG/ML) WAS MIXED WITH 1 MICROL OF RESERVOIR SOLUTION CONTAINING 0.85-1.1 M AMMONIUM SULPHATE IN 0.1 M MES PH 6.5. CRYSTALS WERE IMPROVED BY MICROSEEDING. |