3I3F
Hypothetical protein from Giardia lamblia GL50803_14299
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-01-01 |
Detector | ADSC Quantum-315R CCD |
Wavelength(s) | 0.9795 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 119.900, 119.900, 104.590 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.350 - 1.350 |
R-factor | 0.177 |
Rwork | 0.176 |
R-free | 0.19100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.893 |
Data scaling software | SCALA (3.2.25) |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.410 | 39.410 | 1.420 |
High resolution limit [Å] | 1.350 | 4.270 | 1.350 |
Rmerge | 0.074 | 0.027 | 0.522 |
Total number of observations | 17266 | 55749 | |
Number of reflections | 82643 | ||
<I/σ(I)> | 13.5 | 22.1 | 1.4 |
Completeness [%] | 99.5 | 98.8 | 96.6 |
Redundancy | 6.3 | 6.2 | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | sitting drop, vapor diffusion | 5.5 | 290 | 100 mM Tris, pH 5.5, 25% PEG 3350, 200 mM ammonium acetate, sitting drop, vapor diffusion, temperature 290K |