3ZC8
Crystal Structure of Murraya koenigii Miraculin-Like Protein at 2.2 A resolution at pH 7.0
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | BRUKER |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-01-21 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 101.510, 45.690, 38.780 |
Unit cell angles | 90.00, 95.02, 90.00 |
Refinement procedure
Resolution | 50.560 - 2.240 |
R-factor | 0.19548 |
Rwork | 0.193 |
R-free | 0.24172 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3iir |
RMSD bond length | 0.006 |
RMSD bond angle | 1.174 |
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] | 50.560 | 2.330 |
High resolution limit [Å] | 2.240 | 2.210 |
Rmerge | 0.090 | 0.270 |
Number of reflections | 8649 | |
<I/σ(I)> | 10.3 | 4.4 |
Completeness [%] | 96.3 | 74.9 |
Redundancy | 3.3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 4M AMMONIUM ACETATE, 0.1M BIS-TRIS PROPANE, PH 7.0 |