2AUT
Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-01-31 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 70.737, 84.477, 149.268 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.250 |
| Rwork | 0.151 |
| R-free | 0.19700 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | Partially refined structure of wild-type APHA (PDB code 1Z5G) with all HET atoms (HOH MG etc.) removed and side chain of Lys154 replaced with ALA was used as the starting model. A random error of 0.2A was added to the atomic coordinates of the starting model. |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.000 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (/ TRUNCATE) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.360 |
| High resolution limit [Å] | 2.240 | 2.240 |
| Rmerge | 0.055 | 0.162 |
| Number of reflections | 40671 | |
| <I/σ(I)> | 13.5 | 7.1 |
| Completeness [%] | 94.5 | 91.4 |
| Redundancy | 3.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | vapour diffusion sitting-drop, micro-seeding | 4.7 | 293 | PEG 6000, magnesium chloride, sodium acetate, dihydrogen phosphate , pH 4.7, vapour diffusion sitting-drop, micro-seeding, temperature 293K |
