4HEB
The Crystal structure of Maf protein of Bacillus subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-09-22 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97857 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.550, 85.950, 95.030 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.740 - 2.260 |
R-factor | 0.2155 |
Rwork | 0.215 |
R-free | 0.25000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ex2 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP (10.2..35) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.300 |
High resolution limit [Å] | 2.260 | 2.260 |
Number of reflections | 24272 | |
<I/σ(I)> | 19.7 | |
Completeness [%] | 99.9 | 99.7 |
Redundancy | 7.3 | 0.884 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 295 | 15% PEG 3500, 0.1 M succinate acid pH7.0, vapor diffusion hanging drop, temperature 295K |