5B3Z
Crystal structure of hPin1 WW domain (5-39) fused with maltose-binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-05-25 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.9000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 84.514, 120.433, 110.670 |
Unit cell angles | 90.00, 97.79, 90.00 |
Refinement procedure
Resolution | 49.014 - 2.300 |
R-factor | 0.1834 |
Rwork | 0.181 |
R-free | 0.22410 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf |
RMSD bond length | 0.004 |
RMSD bond angle | 0.834 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 92792 | |
<I/σ(I)> | 10.3 | 1.9 |
Completeness [%] | 95.4 | 89.3 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 1.6M ammonium citrate |