4Q92
1.90 Angstrom resolution crystal structure of apo betaine aldehyde dehydrogenase (betB) G234S mutant from Staphylococcus aureus (IDP00699) with BME-modified Cys289
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-04-17 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 157.363, 156.438, 88.417 |
| Unit cell angles | 90.00, 110.01, 90.00 |
Refinement procedure
| Resolution | 29.500 - 1.900 |
| R-factor | 0.1951 |
| Rwork | 0.194 |
| R-free | 0.22290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4NI4 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.513 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.104 | 0.585 |
| Number of reflections | 155391 | |
| <I/σ(I)> | 17.3 | 2.4 |
| Completeness [%] | 98.8 | 97.9 |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 295 | 7.3 mg/mL protein in 10 mM Tris-HCl, pH 8.3, 500 mM sodium chloride, 5 mM BME against PACT Suite A5/5 (0.1 M SPG, pH 8.0, 25% w/v PEG1500), VAPOR DIFFUSION, SITTING DROP, temperature 295K |
