4XK2
Crystal structure of aldo-keto reductase from Polaromonas sp. JS666
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 | 2014-07-23 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 105.110, 105.110, 479.569 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.1617 |
| Rwork | 0.161 |
| R-free | 0.18470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4jtd |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.261 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.082 | 0.034 | 0.830 |
| Rmeas | 0.090 | 0.037 | 0.910 |
| Rpim | 0.036 | 0.015 | 0.373 |
| Total number of observations | 630404 | ||
| Number of reflections | 106320 | ||
| <I/σ(I)> | 5.8 | 1.9 | |
| Completeness [%] | 100.0 | 99.5 | 100 |
| Redundancy | 5.9 | 5.7 | 5.8 |
| CC(1/2) | 0.998 | 0.702 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 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 3 condition #81 (0.2M NaCl, 0.1M Na citrate, 40%v/v 1,2-propanodiol pH=5.5) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). Before crystallization protein was incubated with 1/50 v/v of 2 mg/ml chymotrypsin solution at 289 K for 3 hours. |
