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 |