5UOG
Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase SMc04462 (SmGhrB) from Sinorhizobium meliloti in apo form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-11-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97924 |
Spacegroup name | H 3 |
Unit cell lengths | 176.583, 176.583, 135.008 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.780 - 2.400 |
R-factor | 0.1381 |
Rwork | 0.136 |
R-free | 0.19040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5j23 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.319 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.440 |
High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
Rmerge | 0.061 | 0.035 | 0.630 |
Rmeas | 0.073 | 0.042 | 0.761 |
Rpim | 0.040 | 0.023 | 0.422 |
Number of reflections | 61899 | 3113 | |
<I/σ(I)> | 9.8 | 2 | |
Completeness [%] | 100.0 | 99.3 | 100 |
Redundancy | 3.2 | 3.2 | 3.2 |
CC(1/2) | 0.996 | 0.685 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 3.5 | 289 | 0.2 ul of 14 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 10% Glycerol, 0.1% Sodium Azide, 0.5 mM TCEP and 5 mM NADPH were mixed with 0.2 ul of the MCSG Suite 3 condition #61 (0.1 M Citric acid pH=3.5, 2 M Ammonium sulfate) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). The protein was crystallized with the His-tag |