3M07
1.4 Angstrom Resolution Crystal Structure of Putative alpha Amylase from Salmonella typhimurium.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-21 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 174.048, 51.534, 57.014 |
| Unit cell angles | 90.00, 101.18, 90.00 |
Refinement procedure
| Resolution | 29.790 - 1.400 |
| R-factor | 0.14913 |
| Rwork | 0.148 |
| R-free | 0.17265 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2bhz |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.448 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.039 | 0.378 |
| Number of reflections | 97228 | |
| <I/σ(I)> | 28.1 | 2.9 |
| Completeness [%] | 99.5 | 96.3 |
| Redundancy | 3.7 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 295 | Protein solution: 8.1 mG/mL, 0.25M Sodium chloride, 0.01M Tris-HCl (pH 8.3); Screen solution: JCSG+, H11, 0.2M Magnesium chloride, 0.1M bis-Tris (pH 5.5), 25% w/v PEG 3350., VAPOR DIFFUSION, SITTING DROP, temperature 295K |
