6CFR
Structure of Human alpha-Phosphomannomutase 1 containing mutation R183I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-07-14 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97917 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 51.910, 51.910, 216.080 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.110 - 2.070 |
R-factor | 0.1736 |
Rwork | 0.169 |
R-free | 0.21210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2fuc |
RMSD bond length | 0.007 |
RMSD bond angle | 1.010 |
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] | 42.110 | 2.126 |
High resolution limit [Å] | 2.070 | 2.070 |
Number of reflections | 18258 | |
<I/σ(I)> | 9.08 | |
Completeness [%] | 96.0 | |
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 |