1FVJ
THE 2.06 ANGSTROM STRUCTURE OF THE H32Y MUTANT OF THE DISULFIDE BOND FORMATION PROTEIN (DSBA)
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 289 |
Detector technology | IMAGE PLATE |
Collection date | 1993-11-05 |
Detector | RIGAKU |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 117.700, 65.100, 76.400 |
Unit cell angles | 90.00, 126.30, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.060 |
R-factor | 0.18 |
Rwork | 0.180 |
R-free | 0.21800 |
Structure solution method | DIFFERENCE FOURIER |
Starting model (for MR) | 1dsb |
RMSD bond length | 0.007 |
RMSD bond angle | 21.980 * |
Data reduction software | R-AXIS (SOFTWARE) |
Data scaling software | R-AXIS |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.250 |
High resolution limit [Å] | 2.060 | 2.060 |
Rmerge | 0.056 | 0.219 |
Total number of observations | 74395 * | |
Number of reflections | 26334 | |
<I/σ(I)> | 17.3 | 3.89 |
Completeness [%] | 91.0 | 84.1 |
Redundancy | 2.8 | 1.98 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 21 * | Martin, J.L., (1993) J.Mol.Biol., 230, 1097. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 20-25 (%(w/v)) | |
2 | 1 | reservoir | MPD | 1 (%) | |
3 | 1 | reservoir | cacodylate | 0.1 (M) | |
4 | 1 | drop | MPD | 1 (%) | |
5 | 1 | drop | PEG8000 | 20-25 (%(w/v)) | |
6 | 1 | drop | cacodylate | 0.1 (M) | |
7 | 1 | drop | DsbA solution | 0.002ml |