5B3W
Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in C2221 form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-06-27 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 1.0000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 97.525, 126.103, 173.523 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.573 - 2.400 |
R-factor | 0.1727 |
Rwork | 0.171 |
R-free | 0.21370 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf |
RMSD bond length | 0.008 |
RMSD bond angle | 1.088 |
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 | 2.440 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 41976 | |
<I/σ(I)> | 14.4 | 3.7 |
Completeness [%] | 99.5 | 99.1 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 2.2 M DL-malic acid |