2P2O
Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-08-07 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97243 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.472, 122.458, 72.541 |
| Unit cell angles | 90.00, 97.88, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.740 |
| R-factor | 0.18631 |
| Rwork | 0.184 |
| R-free | 0.23750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ic7 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.440 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.800 |
| High resolution limit [Å] | 1.740 | 1.740 |
| Number of reflections | 107292 | |
| <I/σ(I)> | 15 | 4.53 |
| Completeness [%] | 92.3 | 65.6 |
| Redundancy | 3.2 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 1 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (10 MG/ML) AND RESERVOIR SOLUTION CONTAINING 0.1 M SODIUM HEPES, 2% V/V PEG400 IN 2.0 M AMMONIUM SULFATE, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
