1AVB
ARCELIN-1 FROM PHASEOLUS VULGARIS L
Experimental procedure
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE DW32 |
Synchrotron site | LURE |
Beamline | DW32 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Collection date | 1995-10 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 85.650, 92.570, 67.280 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.710 - 1.900 |
R-factor | 0.208 |
Rwork | 0.208 |
R-free | 0.24200 |
Structure solution method | MIR, DENSITY MODIFICATION, MOLECULAR REPLACEMENT |
Starting model (for MR) | 1loe |
RMSD bond length | 0.007 |
RMSD bond angle | 27.400 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.700 | 1.950 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.064 | 0.157 |
Number of reflections | 41612 | |
<I/σ(I)> | 11.9 | 7.5 |
Completeness [%] | 97.7 | 93.9 |
Redundancy | 3 | 2.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.8 | 4 * | Mourey, L., (1997) Proteins: Struct.,Funct., Genet., 29, 433. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG400 | 25 (%) | |
3 | 1 | reservoir | ammonium sulfate | 300 (mM) | |
4 | 1 | reservoir | MES | 100 (mM) | pH4.8 or 4.9 |