4QRA
Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 120 |
Detector technology | CCD |
Collection date | 2012-04-06 |
Detector | ADSC QUANTUM 4r |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 113.758, 88.132, 90.512 |
Unit cell angles | 90.00, 90.02, 90.00 |
Refinement procedure
Resolution | 34.860 - 2.290 |
R-factor | 0.18409 |
Rwork | 0.182 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.018 |
RMSD bond angle | 1.843 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 34.860 |
High resolution limit [Å] | 2.290 |
Rmerge | 0.057 |
Number of reflections | 37534 |
<I/σ(I)> | 16.21 |
Completeness [%] | 96.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 289 | 0.02 M calcium chloride, 0.1 M sodium acetate buffer (pH 4.6 to 5), and 30% methyl-2,4-pentanediol (v/v), VAPOR DIFFUSION, SITTING DROP, temperature 289K |