2A22
Structure of Vacuolar Protein Sorting 29 from Cryptosporidium Parvum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-06-06 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 78.841, 78.841, 151.371 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.900 - 2.198 |
R-factor | 0.17024 |
Rwork | 0.168 |
R-free | 0.21391 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w24 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.490 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.900 | 2.280 |
High resolution limit [Å] | 2.198 | 2.198 |
Rmerge | 0.112 | |
Number of reflections | 24958 | |
<I/σ(I)> | 22.89 | 4.45 |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 7.4 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 298 | 22% w/v PEG 400, 100 mM sodium citrate pH 5.6, 200 mM ammonium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |