2VJN
Formyl-CoA transferase mutant variant G260A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-09-29 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 97.260, 97.260, 193.356 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.171 |
| Rwork | 0.169 |
| R-free | 0.21500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1p5h |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.159 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.600 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.150 | 0.500 |
| Number of reflections | 63094 | |
| <I/σ(I)> | 7.2 | 2.5 |
| Completeness [%] | 99.6 | 99.9 |
| Redundancy | 3.3 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |






