5XEP
Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 297 |
Detector technology | CCD |
Collection date | 2006-03-13 |
Detector | MAR CCD 130 mm |
Wavelength(s) | 0.97946 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 130.610, 81.320, 229.330 |
Unit cell angles | 90.00, 105.86, 90.00 |
Refinement procedure
Resolution | 38.270 - 2.600 |
R-factor | 0.1919 |
Rwork | 0.190 |
R-free | 0.23090 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ljy |
RMSD bond length | 0.003 |
RMSD bond angle | 0.759 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHENIX (1.11.1_2575) |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.670 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.085 | 0.486 |
Number of reflections | 71290 | 5288 |
<I/σ(I)> | 13.08 | 2.97 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 3.78 | 3.78 |
CC(1/2) | 0.997 | 0.834 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 20% PEG6000, 1M LiCl2, 0.1M Bicine buffer, pH 9.0 |