1VG0
The crystal structures of the REP-1 protein in complex with monoprenylated Rab7 protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-02-28 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9393 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 64.300, 105.300, 132.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.000 - 2.200 |
R-factor | 0.188 |
Rwork | 0.188 |
R-free | 0.23300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | REP-1 from RabGGTase:REP-1 complex (PDB code 1LTX) |
RMSD bond length | 0.011 |
RMSD bond angle | 1.500 |
Data scaling software | XDS |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.000 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 45399 | |
<I/σ(I)> | 10.19 | 3.61 |
Completeness [%] | 97.6 | 98.5 |
Redundancy | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 298 | 23% PEG 3350, 0.4M diAmmonium Tartrate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |