1SMB
Crystal Structure of Golgi-Associated PR-1 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-10-01 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.8 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 73.662, 73.662, 63.363 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.490 - 1.550 |
Rwork | 0.188 |
R-free | 0.19680 |
Structure solution method | SIRAS |
RMSD bond length | 0.004 |
RMSD bond angle | 1.200 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SHARP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.513 | 1.630 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.077 | 0.278 |
Number of reflections | 28674 | |
<I/σ(I)> | 6.2 | 2.5 |
Completeness [%] | 98.4 | 98.4 |
Redundancy | 6.6 | 6.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 20% (v/v) PEG 8000, 100mM Bis-Tris, 200mM magnesium acetate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |