2AIF
Crystal Structure of High Mobility Like Protein, NHP2, putative from Cryptosporidium parvum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-07-23 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97972 |
Spacegroup name | H 3 |
Unit cell lengths | 90.703, 90.703, 31.275 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 17.900 - 1.895 |
R-factor | 0.20335 |
Rwork | 0.198 |
R-free | 0.27028 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e7k |
RMSD bond length | 0.022 |
RMSD bond angle | 2.279 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.900 | 1.930 |
High resolution limit [Å] | 1.895 | 1.895 |
Rmerge | 0.068 | 0.397 |
Number of reflections | 6861 | |
<I/σ(I)> | 10.7 | 2.01 |
Completeness [%] | 90.0 | 61.3 |
Redundancy | 6.7 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 300 | 1.5 M Sodium Citrate and 0.1M Hepes pH 7.5, VAPOR DIFFUSION, temperature 300K |