3FH4
Crystal Structure of Recombinant Vibrio proteolyticus aminopeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 98 |
Detector technology | IMAGE PLATE |
Collection date | 2008-08-07 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 108.397, 108.397, 93.529 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 26.030 - 1.950 |
R-factor | 0.19294 |
Rwork | 0.191 |
R-free | 0.22776 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2iq6 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.083 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.890 | |
High resolution limit [Å] | 1.950 | 1.950 |
Number of reflections | 23158 | |
<I/σ(I)> | 31.5 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 21 | 21 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | VpAP (0.5 mM) in 10 mM Tris buffer, pH 8.0, containing 10 mM KSCN and 400 mM NaCl was equilibrated with 100 mM Tris buffer, pH 8.0, containing 100 mM KSCN and 4.5 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293K |