1MTN
BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 61 |
Unit cell lengths | 102.450, 102.450, 207.570 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.800 |
R-factor | 0.18 * |
R-free | 0.24800 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cha |
RMSD bond length | 0.013 |
RMSD bond angle | 2.480 |
Data reduction software | MOSFLM |
Phasing software | AMoRE |
Refinement software | TNT |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 * |
High resolution limit [Å] | 2.800 * |
Rmerge | 0.096 |
Total number of observations | 106612 * |
Number of reflections | 27327 |
Completeness [%] | 90.3 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6 | 22 * | pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | alpha-CHT | 10.0 (mg/ml) | |
2 | 1 | drop | BPTI | 4.0 (mg/ml) | |
3 | 1 | drop | magnesium sulfate | 1.0 (M) | |
4 | 1 | drop | sodium acetate | 0.025 (M) |