2B1L
Crystal structure of N-terminal 57 residue deletion mutant of E. coli CcmG protein(residues 58-185)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 293 |
Detector technology | CCD |
Collection date | 2005-03-10 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 37.691, 43.349, 78.986 |
Unit cell angles | 90.00, 94.94, 90.00 |
Refinement procedure
Resolution | 29.140 - 1.900 |
R-factor | 0.193 |
Rwork | 0.193 |
R-free | 0.23100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | structure of E.coli CcmG |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.053 | 0.233 |
Number of reflections | 19846 | |
Completeness [%] | 98.1 | 85.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Seeding | 7.8 | 293 | HEPES buffer, ammonium sulfate, PEG 4000, pH 7.8, Seeding, temperature 293.0K |