1DOA
Structure of the rho family gtp-binding protein cdc42 in complex with the multifunctional regulator rhogdi
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F2 |
Synchrotron site | CHESS |
Beamline | F2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-04-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | H 3 |
Unit cell lengths | 83.940, 83.940, 191.160 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.900 - 2.600 |
R-factor | 0.257 |
Rwork | 0.257 |
R-free | 0.32000 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.640 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.900 * | |
High resolution limit [Å] | 2.600 * | 2.600 * |
Rmerge | 0.057 * | 0.372 * |
Total number of observations | 90533 * | |
Number of reflections | 15454 * | |
Completeness [%] | 100.0 * | 99.8 * |
Redundancy | 5.9 * | 2.4 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 291 | 15% PEG 4000, 100 mM Glutamic Acid, 25 mM MgSO4, 50 mM Tris, 2 mM NaN3, 2 mM LDAO , pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 18K, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 15-20 (%) | |
3 | 1 | reservoir | 25 (mM) | ||
4 | 1 | reservoir | glutamic acid | 100 (mM) | |
5 | 1 | reservoir | lauryldimethylamine-oxide | 2 (mM) | |
6 | 1 | reservoir | Tris-HCl | 100 (mM) |