6NQC

Crystal structure of a peptidase from an acI-B1 Actinobacterium

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	2018-12-08
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	C 2 2 21
Unit cell lengths	44.693, 88.916, 131.311
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.409 - 1.940
R-factor	0.1668
Rwork	0.164
R-free	0.22650
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3l4e
RMSD bond length	0.011
RMSD bond angle	1.023
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHENIX
Refinement software	PHENIX ((1.14_3260: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.500	1.970
High resolution limit [Å]	1.940	1.940
Rmeas	0.088	0.805
Rpim	0.034	0.303
Number of reflections	18380	953
<I/σ(I)>	26.4	3.14
Completeness [%]	91.6	98.8
Redundancy	6.8	6.8
CC(1/2)	0.999	0.915

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	Crystals of enzyme grew after mixing 2 microliters 16 mg/ml protein in buffer (30 mM maleic acid [pH 6.7], 200 mM Na2SO4) with an equal volume of condition 7 (100 mM HEPES-NaOH [pH 7.5], 2% v/v PEG 400, 2 M (NH4)2SO4) from the TOP96 screen (Anatrace) over 500 microliters of the screen solution. 0.5 microliters IZIT crystal dye (Hampton) was added to the crystal-containing droplet after 4 weeks