2XF6
Crystal structure of Bacillus subtilis SPP1 phage gp23.1, a putative chaperone.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-17 |
Detector | MARRESEARCH |
Spacegroup name | P 6 |
Unit cell lengths | 52.400, 52.400, 30.700 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.380 - 2.120 |
R-factor | 0.2056 |
Rwork | 0.191 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 1.060 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | BUSTER-TNT (2.9.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.380 | 2.240 |
High resolution limit [Å] | 2.120 | 2.120 |
Rmerge | 0.060 | 0.240 |
Number of reflections | 2826 | |
<I/σ(I)> | 33.7 | 8.2 |
Completeness [%] | 99.7 | 98.2 |
Redundancy | 11.2 | 8.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.1 M NA HEPES PH7.5 20 PEG 10000 |