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 |
