2GJR
Structure of bacillus halmapalus alpha-amylase without any substrate analogues
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 | 2005-06-30 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.550, 59.040, 209.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.950 - 2.100 |
R-factor | 0.20189 |
Rwork | 0.200 |
R-free | 0.24216 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gjp |
RMSD bond length | 0.008 |
RMSD bond angle | 1.106 |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Number of reflections | 27805 | |
Completeness [%] | 89.9 | 98.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 303 | 10 mM MES-HEPES, boric acid buffer, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 303K |