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.