2I5L
Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2005-07-18 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.9537 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 55.500, 55.500, 55.470 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.500 - 2.550 |
Rwork | 0.227 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1csq |
RMSD bond length | 0.016 |
RMSD bond angle | 1.717 |
Data reduction software | XDS (VERSION June 2005) |
Data scaling software | XSCALE |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.200 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.088 | 0.580 |
Number of reflections | 3223 | |
<I/σ(I)> | 20.14 | 2.8 |
Completeness [%] | 98.2 | 98.6 |
Redundancy | 9.72 | 9.36 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293.15 | protein solution: 20 mM TRIS pH 7.5, 50 mM sodium chloride, 3 mM magnesium chloride, 20.4 mg/ml protein. crystallization buffer: 25 % PEG 3350, 0.2 M sodium carbonate, 0.1 M TRIS HCl pH 8.5. crystallization setup: 0.8 microliter protein solution:0.8 microliter reservoir solution, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |