3M6O
Crystal structure of Arabidopsis thaliana peptide deformylase 1B (AtPDF1B)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-12-16 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.980 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 55.970, 55.940, 148.550 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.970 - 2.000 |
R-factor | 0.22052 |
Rwork | 0.217 |
R-free | 0.28377 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rl4 |
RMSD bond length | 0.022 |
RMSD bond angle | 2.036 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.110 |
High resolution limit [Å] | 2.000 | 1.990 |
Number of reflections | 32457 | |
<I/σ(I)> | 14.48 | 5.1 |
Completeness [%] | 99.0 | 97.3 |
Redundancy | 7.5 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 17% PEG-3350, 0.2M zinc acetate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |