5M8E
Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-2 |
Synchrotron site | MAX II |
Beamline | I911-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-12-05 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.0384 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.880, 71.930, 79.510 |
Unit cell angles | 90.00, 101.93, 90.00 |
Refinement procedure
Resolution | 29.700 - 2.000 |
R-factor | 0.175 |
Rwork | 0.172 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3akh |
RMSD bond length | 0.010 |
RMSD bond angle | 1.030 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.700 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.069 | 0.395 |
<I/σ(I)> | 13.1 | 3.4 |
Completeness [%] | 98.2 | 92.4 |
Redundancy | 3.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | 27 to 29 % PEG 1500, 60 to 140 mM malonate-imidazole-borate (MIB) buffer, pH 4.0 to 4.5 |