4R7P
Human UDP-glucose pyrophosphorylase isoform 1 in complex with UDP-glucose
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-21 |
Detector | ADSC QUANTUM 210 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 138.970, 138.970, 311.620 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.620 - 3.350 |
R-factor | 0.202 |
Rwork | 0.199 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.101 |
Data reduction software | XDS |
Data scaling software | SADABS |
Phasing software | AMoRE |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 47.623 |
High resolution limit [Å] | 3.300 |
Number of reflections | 58213 |
Completeness [%] | 99.7 |
Redundancy | 12.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 281.15 | The protein sample contained 10.3 mg/ml of hUGP, 50 mM HEPES pH 7.5, 5 mM MgCl2, 1 mM EDTA, 20% (w/v) sucrose and 4 mM UDP-Glc. 1 l of the hUGP UDP-Glc complex was mixed 1:1 with the reservoir solution containing 100 mM sodium acetate buffer pH 4.8, 520 mM zinc acetate, 6% (w/v) aminocaproic acid and 75 mM ammonium sulfate. , VAPOR DIFFUSION, SITTING DROP, temperature 281.15K |