2WMB
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 | MARRESEARCH SX-165 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.747, 134.223, 148.236 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.040 - 2.600 |
R-factor | 0.23 |
Rwork | 0.226 |
R-free | 0.29600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h28 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.702 |
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] | 22.040 | 2.690 |
High resolution limit [Å] | 2.500 | 2.550 |
Rmerge | 0.080 | 0.520 |
Number of reflections | 46010 | |
<I/σ(I)> | 10.7 | 1.7 |
Completeness [%] | 95.0 | 89.3 |
Redundancy | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.4 | BUFFER: 10MM HEPES PH 7.0, 100MM NACL. 1.1 TO 1.25M AMMONIUM SULPHATE, 0.7 TO 0.85MM KCL. |