2FM9
Structure of Salmonella SipA residues 48-264
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9A |
Synchrotron site | NSLS |
Beamline | X9A |
Wavelength(s) | 0.979 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 71.080, 71.080, 95.439 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.204 |
Rwork | 0.202 |
R-free | 0.25500 |
Structure solution method | SAD |
RMSD bond length | 0.021 |
RMSD bond angle | 1.784 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.031 | 0.357 |
Number of reflections | 19209 | |
Completeness [%] | 99.0 | 99.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | hanging drops formed from mixing a 1:1 volume ratio of 20mg/ml protein with an equilibration buffer consisting of 20% PEG6000, 20% glycerol, Na-citrate pH 5.6 and 0.01M adenosine-5 -triphosphate disodium salt (ATP) as an additive., VAPOR DIFFUSION, HANGING DROP, temperature 298K |