6X9C
Structure of proline utilization A with L-proline bound in the L-glutamate-gamma-semialdehyde dehydrogenase active site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2018-04-26 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 101.079, 102.253, 127.124 |
Unit cell angles | 90.00, 106.48, 90.00 |
Refinement procedure
Resolution | 48.460 - 1.440 |
R-factor | 0.1811 |
Rwork | 0.180 |
R-free | 0.20530 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 5kf6 |
Data reduction software | XDS |
Data scaling software | Aimless (0.6.3) |
Phasing software | PHENIX |
Refinement software | PHENIX (1.14) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.463 | 48.460 | 1.460 |
High resolution limit [Å] | 1.440 | 7.890 | 1.440 |
Rmerge | 0.059 | 0.024 | 1.263 |
Rmeas | 0.069 | 0.029 | 1.506 |
Rpim | 0.036 | 0.015 | 0.810 |
Total number of observations | 8672 | 44356 | |
Number of reflections | 412199 | 2495 | 13329 |
<I/σ(I)> | 10.9 | 33.9 | 0.8 |
Completeness [%] | 92.4 | 88.2 | 60.4 |
Redundancy | 3.6 | 3.5 | 3.3 |
CC(1/2) | 0.999 | 0.998 | 0.365 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 286 | Crystallization experiments were set up with SmPutA (6 mg/mL) and NADH (10 mM) in a buffer containing 50 mM Tris (pH 8.0), 50 mM NaCl, 5% (w/v) glycerol, and 0.5 mM Tris(2-caboxyethyl)phosphine. Crystals were grown using a reservoir solution containing 19% PEG-3350, 0.2 M ammonium sulfate, 0.1 M magnesium chloride, 0.1 M HEPES (pH 8.0), and 0.1 M sodium formate. Cryobuffer: reservoir supplemented with 15 % PEG-200 and 50 mM L-proline |