3QB0
Crystal structure of Actin-related protein Arp4 from S. cerevisiae complexed with ATP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06SA |
| Synchrotron site | SLS |
| Beamline | X06SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-09 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 61 |
| Unit cell lengths | 118.810, 118.810, 395.660 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.540 - 3.404 |
| R-factor | 0.1929 |
| Rwork | 0.192 |
| R-free | 0.22070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1yag |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.805 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.6.1_357)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.610 |
| High resolution limit [Å] | 3.400 | 3.400 |
| Rmerge | 0.563 | |
| Number of reflections | 43032 | |
| <I/σ(I)> | 11.64 | 3.01 |
| Completeness [%] | 99.5 | 98.4 |
| Redundancy | 5.71 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 27 % PEG2000MME, 0.1 M HEPES-NaOH, 6 % D+-Trehalose, 50 mM Glycine, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
