9IPP

Crystal structure of MERS main protease in complex with carmofur

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL02U1
Synchrotron site	SSRF
Beamline	BL02U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-08-22
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.979183
Spacegroup name	P 21 21 21
Unit cell lengths	79.811, 95.066, 97.441
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	61.740 - 2.260
R-factor	0.195451841086
Rwork	0.194
R-free	0.22694
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.882
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHENIX
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	68.050	2.380
High resolution limit [Å]	2.260	2.260
Rmerge	0.174	1.306
Number of reflections	35490	5105
<I/σ(I)>	12.3
Completeness [%]	100.0
Redundancy	10.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	0.2M Sodium formate, 0.1M BICINE pH8.5 20% PEG5000