3F6T
Crystal structure of aspartate aminotransferase (E.C. 2.6.1.1) (YP_194538.1) from Lactobacillus acidophilus NCFM at 2.15 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-08-27 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.780, 107.750, 119.680 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.921 - 2.150 |
| R-factor | 0.18 |
| Rwork | 0.177 |
| R-free | 0.23800 |
| Structure solution method | SAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.665 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.921 | 29.921 | 2.150 |
| High resolution limit [Å] | 2.150 | 5.060 | 2.100 |
| Rmerge | 0.147 | 0.055 | 0.805 |
| Number of reflections | 63504 | ||
| <I/σ(I)> | 9.204 | ||
| Completeness [%] | 99.9 | 98.8 | 99.9 |
| Redundancy | 3.6 | 3.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.9 | 277 | 0.2000M (NH4)2HPO4, 20.0000% PEG-3350, No Buffer pH 7.9, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |






