2GPW
Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0999 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 62.351, 81.499, 176.649 |
| Unit cell angles | 90.00, 97.69, 90.00 |
Refinement procedure
| Resolution | 29.750 - 2.200 |
| R-factor | 0.192 |
| Rwork | 0.192 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dv1 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | COMO |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.109 | 0.246 |
| Number of reflections | 80638 | |
| <I/σ(I)> | 8.5113 | 4.454 |
| Completeness [%] | 88.5 | 75.8 |
| Redundancy | 2.9 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 294 | 0.1 M Bis-Tris (pH 7.5), 100 mM NaCl, 200 mM trimethylamine N-oxide, 8% (v/v) PEG2000 MME, 4% (v/v) glycerol, 5 mM magnesium chloride, and 2.5 mM DTT, VAPOR DIFFUSION, temperature 294K |
