3FHM
Crystal structure of the CBS-domain containing protein ATU1752 from Agrobacterium tumefaciens
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 | 2008-06-16 |
| Detector | SBC-2 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 1 |
| Unit cell lengths | 53.247, 58.075, 59.056 |
| Unit cell angles | 115.21, 106.15, 94.94 |
Refinement procedure
| Resolution | 30.370 - 2.700 |
| R-factor | 0.19887 |
| Rwork | 0.195 |
| R-free | 0.26164 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | model of protein made from 3rc3 using MrBUMP |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.251 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MrBUMP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.370 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.067 | 0.545 |
| Number of reflections | 19824 | |
| <I/σ(I)> | 18.55 | 1.1 |
| Completeness [%] | 81.7 | 11.6 |
| Redundancy | 4.5 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 0.1 M Tris 8.0, 0.2 M LiSO4, 30% PEG 4K plus 0.015 mg/ml V8 protease. Cryoprotected with Paratone-N oil, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
