6A8Z

Crystal structure of M1 zinc metallopeptidase from Deinococcus radiodurans

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	RRCAT INDUS-2 BEAMLINE PX-BL21
Synchrotron site	RRCAT INDUS-2
Beamline	PX-BL21
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2017-09-01
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.979476
Spacegroup name	P 1
Unit cell lengths	52.371, 57.583, 69.579
Unit cell angles	89.74, 82.30, 67.53

Refinement procedure

Resolution	30.251 - 2.045
R-factor	0.1772
Rwork	0.175
R-free	0.22010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1h19
RMSD bond length	0.007
RMSD bond angle	0.905
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MR-Rosetta
Refinement software	PHENIX ((1.11.1_2575: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.300	2.100
High resolution limit [Å]	2.045	2.050
Rmerge	0.064	0.381
Rmeas	0.076	0.467
Rpim	0.041	0.267
Number of reflections	45670	3200
<I/σ(I)>	14.8	2.9
Completeness [%]	97.3	88.3
Redundancy	3.3	2.6
CC(1/2)	0.997	0.843

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	5.5	294	0.1M Bis-Tris pH 5.5, 0.23M Ammonium formate, 27% PEG3350