3SIB
Crystal structure of URE3-binding protein, wild-type
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-06 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.97946 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 99.699, 99.699, 107.034 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.160 - 1.900 |
| R-factor | 0.161 |
| Rwork | 0.159 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3sia |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.419 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.960 |
| High resolution limit [Å] | 1.900 | 4.350 | 1.900 |
| Rmerge | 0.083 | 0.025 | 0.513 |
| Number of reflections | 21570 | ||
| <I/σ(I)> | 9 | ||
| Completeness [%] | 99.8 | 98.2 | 99.8 |
| Redundancy | 7.9 | 7.6 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | Internal tracking number 202501h3. EnhiA.01648.a.D11 PD00049 (VCID2443) at 12 mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
