2GJP
Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2005-06-05 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.2 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.993, 73.497, 151.094 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.840 - 1.900 |
| R-factor | 0.17445 |
| Rwork | 0.172 |
| R-free | 0.21419 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w9x |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.659 |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 41708 | |
| Completeness [%] | 98.9 | 98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 25 mM acarbose, 18% PEG 5K, 100 mM maltose, 6.4 mM TRIS, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
