1UWY
Crystal structure of human carboxypeptidase M
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-11-15 |
Detector | MARRESEARCH |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 85.830, 85.830, 124.540 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 3.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qmu |
RMSD bond length | 0.012 |
RMSD bond angle | 1.780 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.160 |
High resolution limit [Å] | 2.900 | 3.000 |
Rmerge | 0.061 | 0.271 |
Number of reflections | 19598 | |
Completeness [%] | 97.8 | 99.1 |
Redundancy | 4.2 | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | pH 6.50 |