3L44
Crystal structure of Bacillus anthracis HemL-1, glutamate semialdehyde aminotransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2009-11-13 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.840, 93.920, 105.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.350 - 2.050 |
R-factor | 0.159 |
Rwork | 0.157 |
R-free | 0.19200 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.185 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHENIX |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.120 |
High resolution limit [Å] | 2.050 | 2.050 |
Rmerge | 0.092 | 0.491 |
Number of reflections | 48086 | |
<I/σ(I)> | 17.7 | 4.2 |
Completeness [%] | 99.4 | 100 |
Redundancy | 7.8 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 25% PEG 3350, 100mM Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |