1FP9
STRUCTURE OF AMYLOMALTASE FROM THERMUS THERMOPHILUS HB8 IN SPACE GROUP C2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 1999-10-28 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 104.913, 52.445, 104.908 |
| Unit cell angles | 90.00, 96.42, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.100 |
| R-factor | 0.252 |
| Rwork | 0.239 |
| R-free | 0.29000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fp8 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.031 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.200 | 3.170 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.082 | 0.240 |
| Number of reflections | 10132 | |
| <I/σ(I)> | 8.7 | |
| Completeness [%] | 96.3 | 96.7 |
| Redundancy | 2.03 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | 12% PEG 20000, 100 mM maleate buffer, 0.1% (w/v) maltotriose, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
