2Z3L
complex structure of LF-transferase and peptide A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-5A |
Synchrotron site | Photon Factory |
Beamline | BL-5A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-01-23 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 115.540, 129.998, 38.436 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.890 - 2.750 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.26500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dps |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.850 |
High resolution limit [Å] | 2.750 | 2.750 |
Number of reflections | 15680 | |
<I/σ(I)> | 32.3 | 2.2 |
Completeness [%] | 98.9 | 89 |
Redundancy | 6.7 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 50mM HEPES-Na, 0.7M tri-sodium tartrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |