6VH5
Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.1 |
Synchrotron site | ALS |
Beamline | 5.0.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-21 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9774 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 226.950, 61.250, 120.050 |
Unit cell angles | 90.00, 112.95, 90.00 |
Refinement procedure
Resolution | 41.410 - 2.400 |
R-factor | 0.2083 |
Rwork | 0.207 |
R-free | 0.25060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2QMX_B 3MWB_A 2QMW_A 3LUY_A 4LUB_A |
RMSD bond length | 0.006 |
RMSD bond angle | 0.783 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MR-Rosetta |
Refinement software | PHENIX (1.17.1) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 41.410 | 41.410 | 2.460 |
High resolution limit [Å] | 2.400 | 10.730 | 2.400 |
Rmerge | 0.057 | 0.026 | 0.546 |
Rmeas | 0.065 | 0.029 | 0.619 |
Total number of observations | 263583 | ||
Number of reflections | 59038 | 670 | 4372 |
<I/σ(I)> | 12.82 | 33.51 | 2.33 |
Completeness [%] | 98.4 | 90.4 | 99.3 |
Redundancy | 4.465 | 4.161 | 4.609 |
CC(1/2) | 0.999 | 0.999 | 0.966 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | RigakuReagents PACT screen, condition E12:200mM sodium malonate, dibasic, 20% PEG 3350: BrabA.00146.a.A1.PW25617 at 28.9mg/ml: cryo: 20% EG: tray: 216998 e6, puck gej7-16. |