7BZ3
The mutant variant of PNGM-1. H257 was substituted for alanine to study substrate binding.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 5C (4A) |
| Synchrotron site | PAL/PLS |
| Beamline | 5C (4A) |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-05-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97940 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 79.787, 143.741, 79.760 |
| Unit cell angles | 90.00, 111.82, 90.00 |
Refinement procedure
| Resolution | 48.690 - 2.000 |
| R-factor | 0.2321 |
| Rwork | 0.229 |
| R-free | 0.28640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.722 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0257) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.080 |
| High resolution limit [Å] | 2.000 | 5.540 | 2.040 |
| Rmerge | 0.089 | 0.073 | 0.203 |
| Rmeas | 0.097 | 0.079 | 0.222 |
| Rpim | 0.039 | 0.032 | 0.088 |
| Number of reflections | 103806 | 5285 | 4991 |
| <I/σ(I)> | 12.9 | ||
| Completeness [%] | 97.6 | 99 | 96 |
| Redundancy | 6.2 | 6.3 | 6.2 |
| CC(1/2) | 0.987 | 0.991 | 0.980 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.6 | 287 | 0.1 M Sodium acetate, 20% glycerol, 0.2 M MgCl2 and 7.5% PEG 8000 |
