3AK4
Crystal structure of NADH-dependent quinuclidinone reductase from agrobacterium tumefaciens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E DW |
Temperature [K] | 95 |
Detector technology | IMAGE PLATE |
Collection date | 2008-08-03 |
Detector | RIGAKU RAXIS VII |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 62.550, 127.300, 62.480 |
Unit cell angles | 90.00, 110.40, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.151 |
Rwork | 0.149 |
R-free | 0.19100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1geg |
RMSD bond length | 0.019 |
RMSD bond angle | 1.518 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 61144 | |
<I/σ(I)> | 20.6 | 7.5 |
Completeness [%] | 98.1 | 91.4 |
Redundancy | 3.5 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 24% PEG3350, 100MM HEPES, 200MM AMMONIUM ACETATE, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |