1EX2
CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 5ID-B |
Synchrotron site | APS |
Beamline | 5ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-09-05 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.660, 86.010, 93.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.850 |
Rwork | 0.195 |
R-free | 0.22300 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.068 | 0.449 |
Total number of observations | 186600 * | |
Number of reflections | 43834 | |
<I/σ(I)> | 17 | |
Completeness [%] | 99.4 | 96.3 |
Redundancy | 4.3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
3 | 1 | reservoir | PEG8000 | 8 (%) |