3WOA
Crystal structure of lambda repressor (1-45) fused with maltose-binding protein
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 MX-225 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 150.865, 52.622, 58.271 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.682 - 2.000 |
| R-factor | 0.1599 |
| Rwork | 0.158 |
| R-free | 0.19390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1anf |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.120 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 32189 | |
| <I/σ(I)> | 15.1 | 11.3 |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 6.8 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 1.6M DL-Malic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
