3K48
Crystal structure of APRIL bound to a peptide
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 | 2005-04-07 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 100.811, 84.771, 55.562 |
Unit cell angles | 90.00, 99.45, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.800 |
R-factor | 0.21169 |
Rwork | 0.205 |
R-free | 0.26690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Chain A from pdb 1xu1 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.252 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Number of reflections | 11453 | |
<I/σ(I)> | 12.4 | 2.5 |
Completeness [%] | 99.6 | 98.4 |
Redundancy | 3.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 292 | 2ul drops of protein (5 mg/mg. at pH 9.7) was added to 2 uL of 4M formate. Crystals formed immediately, VAPOR DIFFUSION, HANGING DROP, temperature 292K |