6D97
Structure of aldehyde dehydrogenase 12 (ALDH12) from Zea mays
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 | 2016-11-03 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 160.642, 123.737, 103.707 |
Unit cell angles | 90.00, 105.62, 90.00 |
Refinement procedure
Resolution | 46.680 - 2.200 |
R-factor | 0.1668 |
Rwork | 0.165 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4mpy |
RMSD bond length | 0.003 |
RMSD bond angle | 0.676 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.32) |
Phasing software | BALBES |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 61.870 | 61.870 | 2.240 |
High resolution limit [Å] | 2.200 | 12.050 | 2.200 |
Rmerge | 0.092 | 0.028 | 1.007 |
Rmeas | 0.109 | 0.034 | 1.241 |
Rpim | 0.057 | 0.018 | 0.712 |
Total number of observations | 2159 | 12672 | |
Number of reflections | 98196 | 618 | 4545 |
<I/σ(I)> | 11.6 | 37.8 | 1.1 |
Completeness [%] | 99.3 | 95.9 | 93.4 |
Redundancy | 3.5 | 3.5 | 2.8 |
CC(1/2) | 0.996 | 0.998 | 0.456 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | BATCH MODE | 293 | 50% v/v of a precipitant mixture containing 25% v/v 2-methyl-2,4-pentanediol, 25% w/v polyethylene glycol 1000, and 25% w/v polyethylene glycol 3350; and 0.1 M Tris/bicine pH 8.5 |