1VYJ
Structural and biochemical studies of human PCNA complexes provide the basis for association with CDK/cyclin and rationale for inhibitor design
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7A |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7A |
| Temperature [K] | 100 |
| Collection date | 2001-08-15 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 119.101, 119.101, 305.817 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 14.000 - 2.800 |
| R-factor | 0.17897 |
| Rwork | 0.176 |
| R-free | 0.25600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1axc |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.090 | 0.620 |
| Number of reflections | 62908 | |
| <I/σ(I)> | 7.5 | 1 |
| Completeness [%] | 98.7 | 98.6 |
| Redundancy | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 2.7M AS, HEPES PH8, pH 8.00 |
