3OOV
Crystal structure of a methyl-accepting chemotaxis protein, residues 122 to 287
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97911 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 60.132, 60.132, 363.131 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 60.520 - 2.200 |
R-factor | 0.24022 |
Rwork | 0.237 |
R-free | 0.30485 |
Structure solution method | SAD |
RMSD bond length | 0.023 |
RMSD bond angle | 1.957 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 60.520 |
High resolution limit [Å] | 2.200 |
Completeness [%] | 99.4 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 289 | 10% w/v PEG 3000, 0.10M phosphate-citrate, pH4.2, 0.20M NaCl. (Wizard II, #36) cryoprotectant: included all of above, in addition to 25% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 289K |