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. |
