6CFU
Structure of Human alpha-Phosphomannomutase 1 containing mutations R180K and R183K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-08-21 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9791 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 50.650, 50.650, 213.410 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.280 - 2.244 |
R-factor | 0.2223 |
Rwork | 0.217 |
R-free | 0.27390 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2fuc |
RMSD bond length | 0.008 |
RMSD bond angle | 1.134 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.280 | 2.320 |
High resolution limit [Å] | 2.240 | 2.240 |
Number of reflections | 13960 | |
<I/σ(I)> | 9.62 | |
Completeness [%] | 98.4 | |
Redundancy | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 290 | 20% polyethylene glycol 3350, 0.15 M DL-malate, pH 7.0, 50 mM MgCl2, and 8 mM beta-mercaptoethanol |