5C1E
Crystal Structure of the Pectin Methylesterase from Aspergillus niger in Penultimately Deglycosylated Form (N-acetylglucosamine Stub at Asn84)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 123 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-11-04 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 74.614, 113.543, 88.765 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.160 - 1.750 |
| R-factor | 0.1725 |
| Rwork | 0.171 |
| R-free | 0.20150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xg2 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.305 |
| Data reduction software | CrystalClear |
| Data scaling software | d*TREK |
| Phasing software | MrBUMP |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.160 | 1.800 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.084 | 0.366 |
| Number of reflections | 36656 | |
| <I/σ(I)> | 4.5 | 3.1 |
| Completeness [%] | 95.6 | 89.6 |
| Redundancy | 3.94 | 3.71 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 3.6 | 294 | Protein (6.5 mg/mL) in 50-100 mM acetate buffer mixed 1:1 with 1.9 M ammonium sulfate, 100 mM sodium acetate, pH 3.6 |
