3TUU
Structure of dihydrodipicolinate synthase from the common grapevine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2011-01-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 |
Unit cell lengths | 70.550, 78.900, 135.350 |
Unit cell angles | 93.19, 95.02, 100.61 |
Refinement procedure
Resolution | 57.170 - 2.200 |
R-factor | 0.18205 |
Rwork | 0.180 |
R-free | 0.22745 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.337 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 134.470 | 2.257 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 133745 | |
Completeness [%] | 97.3 | 96.98 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.2 | 293 | diffracting crystal were obtained by mixing 2 uL of protein solution (10 mg/mL) with 2 uL of reservoir solution: 0.1 M BTP, 0.2 M NaBr, 20 % (w/v) PEG 3350, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |