Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 283 |
Detector technology | IMAGE PLATE |
Collection date | 1990-07-07 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 157.200, 157.200, 201.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 1.600 |
R-factor | 0.211 |
Rwork | 0.211 |
Structure solution method | MIR STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL |
RMSD bond length | 0.010 |
RMSD bond angle | 24.100 * |
Data reduction software | WEIS |
Data scaling software | SCALE |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.670 |
High resolution limit [Å] | 1.500 | 1.600 |
Rmerge | 0.069 | |
Total number of observations | 1131480 * | |
Number of reflections | 277449 | |
Completeness [%] | 49 | |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | Andersson, I., (1983) J. Biol. Chem., 258, 14088. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | ||
2 | 1 | drop | 0.05 (M) | ||
3 | 1 | drop | PEG6000 | 8-15 (%) | |
4 | 1 | reservoir | 0.05 (M) | ||
5 | 1 | reservoir | PEG6000 | 8-15 (%) | |
6 | 1 | reservoir | 0.1 (M) |