2C30
Crystal Structure Of The Human P21-Activated Kinase 6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-09-03 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.781, 66.674, 96.999 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 54.960 - 1.600 |
R-factor | 0.198 |
Rwork | 0.197 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 2BVA 1yhw 1yhv 1f3m |
RMSD bond length | 0.016 |
RMSD bond angle | 1.610 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.000 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.080 | 0.570 |
Number of reflections | 177870 | |
<I/σ(I)> | 11.1 | 2.1 |
Completeness [%] | 98.8 | 93.6 |
Redundancy | 3.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 1.60M MGSO4 0.1M MES PH 6.5 SITTING DROPS, 150NL AND 50NL PROTEIN AND RESERVOIR MIX. |