1XRM
Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-04-15 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.970, 61.920, 80.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 16.710 - 2.700 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.28200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1mtz |
RMSD bond length | 0.008 |
RMSD bond angle | 1.000 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((TRUNCATE)) |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.000 | 2.870 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 7564 | |
<I/σ(I)> | 14 | |
Completeness [%] | 98.9 | 60.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | PEG 6000, Bis-Tris, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |