1BN5
HUMAN METHIONINE AMINOPEPTIDASE 2
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F1 |
| Synchrotron site | CHESS |
| Beamline | F1 |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 1998-06 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 90.490, 99.380, 101.590 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.800 |
| R-factor | 0.183 * |
| Rwork | 0.183 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xgs |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.026 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.500 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.069 | 0.149 |
| Total number of observations | 154879 * | |
| Number of reflections | 42299 | |
| <I/σ(I)> | 14.7 | 6.8 |
| Completeness [%] | 99.0 | 99.4 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.2 * | 4 * | pH 5.4 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | |
| 3 | 1 | drop | glycerol | 10 (%) | |
| 4 | 1 | drop | 100 (mM) | ||
| 5 | 1 | reservoir | t-butanol | 15-30 (%) | |
| 6 | 1 | reservoir | sodium citrate | 33-100 (mM) |
