3ZC9
Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 4.6
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-01-22 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.620, 45.420, 38.790 |
Unit cell angles | 90.00, 94.87, 90.00 |
Refinement procedure
Resolution | 50.630 - 2.240 |
R-factor | 0.19352 |
Rwork | 0.191 |
R-free | 0.23798 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3iir |
RMSD bond length | 0.006 |
RMSD bond angle | 1.235 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.630 | 2.330 |
High resolution limit [Å] | 2.210 | 2.210 |
Rmerge | 0.070 | 0.220 |
Number of reflections | 7985 | |
<I/σ(I)> | 13.7 | 5.7 |
Completeness [%] | 90.0 | 60.3 |
Redundancy | 3.5 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.6 | 4M AMMONIUM ACETATE, 0.1M SODIUM ACETATE TRIHYDRATE PH 4.6 |