5UNN
Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc02828 (SmGhrA) from Sinorhizobium meliloti in apo form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-18 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97856 |
Spacegroup name | I 41 |
Unit cell lengths | 128.592, 128.592, 122.847 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.1482 |
Rwork | 0.147 |
R-free | 0.17420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4z0p |
RMSD bond length | 0.011 |
RMSD bond angle | 1.369 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.030 |
High resolution limit [Å] | 2.000 | 5.430 | 2.000 |
Rmerge | 0.108 | 0.046 | 0.902 |
Rmeas | 0.117 | 0.050 | 0.986 |
Rpim | 0.044 | 0.019 | 0.389 |
Number of reflections | 67353 | ||
<I/σ(I)> | 6.9 | 1.7 | |
Completeness [%] | 100.0 | 99.8 | 100 |
Redundancy | 6.9 | 6.9 | 6.6 |
CC(1/2) | 0.998 | 0.615 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 289 | 0.2 ul of 12 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide and 0.5 mM TCEP were mixed with 0.2 ul of the MCSG suite I condition # 88 (0.1 M Sodium citrate pH=5.6, 20% v/v 2-Propanol, 20% w/v PEG 4000 ) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci) |