6IFG

Crystal structure of M1 zinc metallopeptidase E323A mutant bound to Tyr-ser-ala substrate 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	2018-07-28
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.979470
Spacegroup name	P 1
Unit cell lengths	51.598, 57.594, 69.321
Unit cell angles	89.77, 82.14, 67.80

Refinement procedure

Resolution	24.137 - 1.900
R-factor	0.1821
Rwork	0.180
R-free	0.21420
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6a8z
RMSD bond length	0.005
RMSD bond angle	0.796
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.830	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.052	0.352
Rmeas	0.065	0.446
Rpim	0.039	0.269
Number of reflections	56301	3603
<I/σ(I)>	14.2	3.2
Completeness [%]	97.7	96.3
Redundancy	2.7	2.7
CC(1/2)	0.997	0.865

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	5.5	294	0.2M Ammonium formate, 0.1M Bis-tris pH 5.5, 25% PEG 3350