8FOL

The structure of a crystallizable variant of E. coli pyruvate formate-lyase activating enzyme bound to SAM, alternate crystal form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2016-08-14
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.542
Spacegroup name	P 21 21 21
Unit cell lengths	49.653, 59.011, 96.792
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.370 - 2.650
R-factor	0.1957
Rwork	0.195
R-free	0.21420
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.786
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.370	2.745
High resolution limit [Å]	2.650	2.650
Rmerge	0.125	0.841
Rmeas	0.142	0.954
Rpim	0.066	0.441
Number of reflections	8650	752
<I/σ(I)>	10.26	1.29
Completeness [%]	97.7	88.01
Redundancy	4.3	4.2
CC(1/2)	0.996	0.710

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	300	4 uL of protein (10 mg/mL PFL-AE-CCR8 in 12.5 mM HEPES, 200 mM KCl, with 3.65 mM SAM, 1.2 mM WT 7-mer PFL peptide, 0.13% glycerol, and 1 mM DTT) were combined with 1 uL of crystallization reservoir solution (18% PEG 3350, 100 mM HEPES, pH 7.5) in hanging drop format over 50 uL of crystallization reservoir solution.