1CTQ
STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 1998-06-16 |
Detector | SIEMENS HI-STAR |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 39.670, 39.670, 158.409 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.260 |
R-factor | 0.172 |
Rwork | 0.172 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5p21 |
RMSD bond length | 0.010 |
RMSD bond angle | 2.290 |
Data scaling software | XDS |
Phasing software | X-PLOR |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.350 |
High resolution limit [Å] | 1.260 | 1.260 |
Rmerge | 0.027 | 0.116 |
Number of reflections | 35100 | |
<I/σ(I)> | 28.9 | 6.7 |
Completeness [%] | 86.5 | 58.8 |
Redundancy | 3 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.6 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 28 % PEG 400, 10MM MGCL 264MM TRIS/HCL, PH 7.6, pH 7.60, micro-batch, temperature 18K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 12.5-15 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 64 (mM) | |
3 | 1 | 1 | 10 (mM) | ||
4 | 1 | 1 | dithiothreitol | 10 (mM) | |
5 | 1 | 1 | PEG400 | 28 (%(v/v)) |