4GPZ
Crystal structure of human B type phosphoglycerate mutase H11 phosphorylated form
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] | 180 |
Detector technology | CCD |
Collection date | 2011-10-11 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97918 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 77.360, 81.174, 90.381 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 60.390 - 1.650 |
R-factor | 0.18647 |
Rwork | 0.185 |
R-free | 0.21382 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yfk |
RMSD bond length | 0.025 |
RMSD bond angle | 2.471 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASES |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 60.478 | 2.240 | 1.710 |
High resolution limit [Å] | 1.650 | 2.080 | 1.650 |
Number of reflections | 72475 | ||
Completeness [%] | 100.0 | 100 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | PEG3350, MES, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |