5FAX
Structure of subtilase SubHal from Bacillus halmapalus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-03-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.933 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.224, 99.935, 96.749 |
Unit cell angles | 90.00, 103.52, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.21522 |
Rwork | 0.215 |
R-free | 0.30300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Complex of SubHal with CI2A inhibitor PDB ID 5FBZ |
RMSD bond length | 0.017 |
RMSD bond angle | 1.678 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK (1.97.2) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.101 | 0.268 |
Number of reflections | 41891 | |
<I/σ(I)> | 6 | 2.4 |
Completeness [%] | 74.0 | 49.1 |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | Protein concentration 24 mg ml-1 in 50 mM sodium cacodylate buffer, pH 6.5, 2 mM CaCl2 and 100 mM NaCl. The enzyme was crystallised by hanging drop vapour diffusion in drops containing 1 microliter of protein and 1 microliter of reservoir solution over 0.5 ml of reservoir: Hampton Screen 2 no. 23 (10% dioxane, 0.1 M 2-(N-Morpholino)-ethanesulphonic acid (MES) buffer, pH 6.5, 1.6 M ammonium sulphate). Clusters of elongated plates appeared after several days. |