2MAT
E.COLI METHIONINE AMINOPEPTIDASE AT 1.9 ANGSTROM RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-10 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 39.299, 67.683, 48.863 |
Unit cell angles | 90.00, 111.24, 90.00 |
Refinement procedure
Resolution | 35.500 - 1.900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mat |
RMSD bond length | 0.012 |
RMSD bond angle | 2.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | TNT (5F PRERELEASE) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.500 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.077 * | 0.251 * |
Total number of observations | 94123 * | |
Number of reflections | 18444 | |
<I/σ(I)> | 22.7 | 6.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.1 | drop consists of 1:1 mixture of well and protein solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | drop | N-octanoyl sucrose | 48.8 (mM) | |
3 | 1 | reservoir | PEG4000 | 24-26 (%) | |
4 | 1 | reservoir | HEPES | 0.1 (M) | |
5 | 1 | reservoir | 2 (mM) |