7LNM
Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclopentene-1-carboxylic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-10-21 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.9787 |
Spacegroup name | P 32 |
Unit cell lengths | 115.720, 115.720, 188.021 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 36.480 - 2.000 |
R-factor | 0.159 |
Rwork | 0.158 |
R-free | 0.18600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1oat |
Data reduction software | xia2 |
Data scaling software | xia2 |
Phasing software | PHASER |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 68.560 | 68.560 | 2.030 |
High resolution limit [Å] | 2.000 | 10.950 | 2.000 |
Rmerge | 0.118 | 0.070 | 1.086 |
Rmeas | 0.136 | 0.082 | 1.284 |
Rpim | 0.068 | 0.042 | 0.678 |
Total number of observations | 749788 | 4224 | 33035 |
Number of reflections | 190270 | 1136 | 9377 |
<I/σ(I)> | 4.6 | 7.6 | 1.3 |
Completeness [%] | 100.0 | 97.1 | 100 |
Redundancy | 3.9 | 3.7 | 3.5 |
CC(1/2) | 0.993 | 0.987 | 0.376 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 8000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8. |