5TF2
CRYSTAL STRUCTURE OF THE WD40 DOMAIN OF THE HUMAN PROLACTIN REGULATORY ELEMENT-BINDING PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-06-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.92045 |
| Spacegroup name | P 64 2 2 |
| Unit cell lengths | 160.708, 160.708, 83.014 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.800 |
| R-factor | 0.19 |
| Rwork | 0.189 |
| R-free | 0.21400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1erj |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.305 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 6.030 | 2.800 |
| Rmerge | 0.107 | 0.046 | 0.779 |
| Rmeas | 0.111 | ||
| Rpim | 0.031 | ||
| Total number of observations | 198545 | ||
| Number of reflections | 16070 | ||
| <I/σ(I)> | 6.3 | ||
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 12.4 | 11.1 | 12.7 |
| CC(1/2) | 0.999 | 0.898 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | PREB protein was mixed with elastase at 1:1000 (w/w) ratio before setting up crystallization. Crystals were grown at 293 K using the sitting drop method by mixing 0.5 uL protein with 0.5 uL well solution consisting of 1.4M Malonate, pH 7.0. The crystals were cryoprotected by immersion in Paratone. |
