1A8T
METALLO-BETA-LACTAMASE IN COMPLEX WITH L-159,061
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1997-02-18 |
Detector | SIEMENS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.360, 170.230, 40.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.550 |
R-factor | 0.181 |
R-free | 0.31900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a7t |
RMSD bond length | 0.018 |
RMSD bond angle | 0.043 |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | MERLOT |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.710 |
High resolution limit [Å] | 2.550 | 2.550 |
Rmerge | 0.077 | 0.125 |
Number of reflections | 12599 | 1468 * |
<I/σ(I)> | 12.1 | 2.4 |
Completeness [%] | 75.0 | 53.8 |
Redundancy | 1.93 | 1.65 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.6 | PROTEIN WAS CRYSTALLIZED FROM 28% PEG 4000, 100 MM SODIUM CHLORIDE, 100 MM SODIUM CACODYLATE BUFFER, PH 6.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium cacodylate | 100 (mM) | |
2 | 1 | reservoir | 100 (mM) | ||
3 | 1 | reservoir | sodium acetate | 10 (mM) | |
4 | 1 | reservoir | PEG4000 | 28 (%(w/v)) |