3CP3
Crystal structure of conserved protein of unknown function DIP1874 from Corynebacterium diphtheriae
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 | 2007-06-04 |
| Detector | SBC-3 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | I 41 |
| Unit cell lengths | 59.374, 59.374, 98.948 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.680 - 2.000 |
| R-factor | 0.19 |
| Rwork | 0.188 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SAD phased model of the L37M mutant of the same protein P1 space group |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.760 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.900 | 2.050 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.049 | 0.297 |
| Number of reflections | 11597 | |
| <I/σ(I)> | 12.3 | 5.77 |
| Completeness [%] | 97.3 | 76.4 |
| Redundancy | 11.7 | 8.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.7 | 295 | 30% PEG 8000, 0.1 M Acetate pH 4.5, 0.2 M Lithium sulfate, pH 4.7, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
