4JMX
Structure of LD transpeptidase LdtMt1 in complex with imipenem
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-31 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 67.397, 67.397, 119.564 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.950 - 2.550 |
R-factor | 0.16444 |
Rwork | 0.161 |
R-free | 0.23317 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.403 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.550 | 2.550 |
Number of reflections | 9506 | |
Completeness [%] | 99.8 | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | protein concentration of 3.5 mg/mL and 1.24 M sodium phosphate and 0.16 M potassium phosphate, 10 mM TCEP, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |