1VDD
Crystal structure of recombinational repair protein RecR
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 6B |
| Synchrotron site | PAL/PLS |
| Beamline | 6B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-11-20 |
| Detector | BRUKER PROTEUM 300 |
| Wavelength(s) | 0.97182, 0.97936, 0.97950, 0.99999, 1.00812, 1.00883, 1.00921 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 106.218, 121.386, 154.993 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.390 - 2.500 |
| R-factor | 0.233 |
| Rwork | 0.233 |
| R-free | 0.30100 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | SMART |
| Data scaling software | SAINTPLUS |
| Phasing software | SOLVE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.390 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 33796 | |
| <I/σ(I)> | 2.63 | |
| Completeness [%] | 97.2 | 97.3 |
| Redundancy | 6.1 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | PEG 1000, calcium acetate, 1,3-butanediol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
