2WMA
Structural and thermodynamic consequences of cyclization of peptide ligands for the recruitment site of cyclin A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.792, 131.853, 146.883 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.800 |
R-factor | 0.21476 |
Rwork | 0.211 |
R-free | 0.28514 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h28 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.488 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.130 | 0.570 |
Number of reflections | 44032 | |
<I/σ(I)> | 8.3 | 1.6 |
Completeness [%] | 99.4 | 92.5 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 10MM HEPES PH 7, 100MM NACL 1.1 TO 1.25M AMMONIUM SULPHATE, 0.7 TO 0.85M KCL |