5VPU
Crystal Structure of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase bound to 3-phosphoglycerate, from Acinetobacter baumannii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-04-29 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97856 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.940, 82.090, 72.410 |
Unit cell angles | 90.00, 97.64, 90.00 |
Refinement procedure
Resolution | 41.045 - 1.500 |
R-factor | 0.1355 |
Rwork | 0.135 |
R-free | 0.16400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1o98 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.108 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHENIX |
Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 41.045 | 41.045 | 1.540 |
High resolution limit [Å] | 1.500 | 6.710 | 1.500 |
Rmerge | 0.048 | 0.034 | 0.151 |
Rmeas | 0.052 | 0.037 | 0.169 |
Total number of observations | 517771 | ||
Number of reflections | 84305 | 986 | 6026 |
<I/σ(I)> | 22.98 | 38.03 | 9.05 |
Completeness [%] | 99.0 | 99.4 | 95.5 |
Redundancy | 6.142 | 6.508 | 5.148 |
CC(1/2) | 0.999 | 0.999 | 0.987 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | MCSG1 F2: 0.2 M Ammonium Acetate 0.1 M Bis-Tris: HCl, pH 6.5 25 % (w/v) PEG 3350 +3mM 3-phosphoglycerate cryo:15% Ethylene glycol PS38071 24.7mg/mL, 0.4+0.4 puck frn7-12 |