7S77
Crystal structure of the G391V variant of human PGM-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2018-11-15 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000001 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 171.050, 171.050, 100.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.180 - 2.800 |
R-factor | 0.1956 |
Rwork | 0.193 |
R-free | 0.25180 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 5epc |
RMSD bond length | 0.009 |
RMSD bond angle | 1.095 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHENIX |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.180 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.160 | 2.240 |
Rmeas | 0.160 | |
Rpim | 0.045 | 0.830 |
Number of reflections | 37211 | 3643 |
<I/σ(I)> | 15.44 | 1.24 |
Completeness [%] | 99.5 | 99.95 |
Redundancy | 13.2 | 13.7 |
CC(1/2) | 0.999 | 0.512 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | condition 2-33 of the Morpheus crystal screen (Molecular Dimensions) at a protein concentration of 10 mg/mL from a hanging drop of 1 ml protein and 4 ml well buffer. Condition 2-33 contains 0.1 M of a carboxylic acid mixture (0.2 M sodium formate, 0.2 M ammonium acetate, 0.2 M sodium citrate tribasic dihydrate, 0.2 M sodium potassium tartrate tetrahydrate, and 0.2 M sodium oxamate), 0.1 M of a buffer system at pH 8.5 (Tris base and BICINE), and a 30% v/v precipitant mix (40% v/v PEG 500 MME and 20% w/v PEG 20000) |