4XAP
Crystal structure of aldo-keto reductase from Sinorhizobium meliloti 1021
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 | 2014-11-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.533, 78.068, 79.073 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.210 |
| R-factor | 0.1634 |
| Rwork | 0.160 |
| R-free | 0.22460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4pmj |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.720 |
| 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 | 2.240 |
| High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
| Rmerge | 0.072 | 0.037 | 0.692 |
| Rmeas | 0.080 | 0.042 | 0.768 |
| Rpim | 0.035 | 0.019 | 0.327 |
| Total number of observations | 65764 | ||
| Number of reflections | 14216 | ||
| <I/σ(I)> | 17.6 | 2.1 | |
| Completeness [%] | 98.7 | 95.2 | 98.7 |
| Redundancy | 4.6 | 4.3 | 4.5 |
| CC(1/2) | 0.998 | 0.805 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.2 ul of 15 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 PEG/Ion HT condition #70 (0.2M Ammonium Citrate Tribasic anhydrous, 20% w/v PEG 3350 pH=7) 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 1 mg/ml TEV solution at 289 K for 1 hour |
