5CNX
Crystal structure of Xaa-Pro aminopeptidase from Escherichia coli K12
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | RRCAT INDUS-2 BEAMLINE PX-BL21 |
| Synchrotron site | RRCAT INDUS-2 |
| Beamline | PX-BL21 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-01-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97947 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 224.202, 224.202, 74.636 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.897 - 2.600 |
| R-factor | 0.2199 |
| Rwork | 0.219 |
| R-free | 0.24030 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3q6d |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.995 |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.900 | 2.660 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.109 | 0.673 |
| Number of reflections | 66134 | |
| <I/σ(I)> | 10.8 | 2.1 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 293 | Crystallization solution: 1.4 M Sodium Citrate, 0.1 M Sodium Cacodylate pH 6.6, 10% glycerol, 1 mM ZnCl2 Protein solution: 20 mM TrisHCl, 200 mM NaCl |
