1P3D
Crystal Structure of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) in Complex with UMA and ANP.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-09-30 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.920, 87.328, 86.113 |
| Unit cell angles | 90.00, 104.86, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.700 |
| R-factor | 0.16953 |
| Rwork | 0.168 |
| R-free | 0.19400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1p31 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.130 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.046 | 0.540 * |
| Total number of observations | 488589 * | |
| Number of reflections | 113461 | |
| <I/σ(I)> | 13.4 | 2.47 |
| Completeness [%] | 96.6 | 90.5 |
| Redundancy | 4.31 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 | 20 * | PEG 4000, isopropanol, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | UNAM | 5 (mM) | |
| 3 | 1 | drop | Ala | 5 (mM) | |
| 4 | 1 | drop | Mn2+ | 5 (mM) | |
| 5 | 1 | drop | AMP-PNP | 5 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 20 (%) | |
| 7 | 1 | reservoir | isopropanol | 10 (%) | |
| 8 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
