7UNP
Crystal structure of the CelR catalytic domain and CBM3c
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-07-25 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.978720 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.751, 91.076, 66.909 |
Unit cell angles | 90.00, 110.99, 90.00 |
Refinement procedure
Resolution | 36.800 - 2.000 |
R-factor | 0.1619 |
Rwork | 0.160 |
R-free | 0.20700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k72 |
Data reduction software | XDS (20200417) |
Data scaling software | XSCALE (20200417) |
Phasing software | PHASER (2.8.3) |
Refinement software | PHENIX (1.20.1-4487) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 36.800 | 36.800 | 2.050 |
High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
Rmerge | 0.118 | 0.027 | 0.644 |
Rmeas | 0.164 | 0.038 | 0.891 |
Total number of observations | 152259 | ||
Number of reflections | 77040 | 861 | 5668 |
<I/σ(I)> | 6.02 | 20.86 | 1.34 |
Completeness [%] | 96.0 | 94.5 | 95.9 |
Redundancy | 1.976 | 1.926 | 1.987 |
CC(1/2) | 0.987 | 0.996 | 0.562 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | Crystals were grown in a MRC SD2 plate set by a SPT Labtech Mosquito crystallization robot. 200 nL of protein at 29.5 mg/mL was mixed with 200 nL of reservoir solution, consisting of 0.1 M sodium citrate buffer, pH 5, 20% w/v PEG 6000. Vapor diffusion against 50 microliters of reservoir. |