4RM3
Crystal structure of a benzoate coenzyme A ligase with 2-Furoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-04-16 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.637, 95.110, 95.330 |
| Unit cell angles | 90.00, 104.88, 90.00 |
Refinement procedure
| Resolution | 33.090 - 1.760 |
| R-factor | 0.18576 |
| Rwork | 0.184 |
| R-free | 0.22927 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2v7b |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.027 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | Mol (Rep) |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.790 |
| High resolution limit [Å] | 1.760 | 1.760 |
| Rmerge | 0.111 | 0.570 |
| Number of reflections | 93457 | |
| <I/σ(I)> | 16.91 | 1.61 |
| Completeness [%] | 98.5 | 89.89 |
| Redundancy | 3.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 15 % PEG 3350, 0.1 M Tris pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
