1VM6
Crystal structure of Dihydrodipicolinate reductase (TM1520) from Thermotoga maritima at 2.27 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-05-24 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 133.077, 109.217, 112.602 |
Unit cell angles | 90.00, 119.23, 90.00 |
Refinement procedure
Resolution | 29.030 - 2.270 |
R-factor | 0.17334 |
Rwork | 0.171 |
R-free | 0.21256 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1arz |
RMSD bond length | 0.014 |
RMSD bond angle | 1.596 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.030 | 2.390 |
High resolution limit [Å] | 2.270 | 2.270 |
Number of reflections | 61963 | |
<I/σ(I)> | 10.8 | 2 |
Completeness [%] | 47.8 | 38.4 |
Redundancy | 3.6 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 4.5 | 293 | 20.0% PEG-400, 0.2M Ca(OAc)2, 0.1M Acetate pH 4.5, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K |