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 |