9HQT

SFX structure of cytochrome c prime beta from Methylococcus capsulatus (Bath)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	FREE ELECTRON LASER
Source details	SACLA BEAMLINE BL2
Synchrotron site	SACLA
Beamline	BL2
Temperature [K]	300
Detector technology	CCD
Collection date	2019-06-26
Detector	MPCCD
Wavelength(s)	1.127
Spacegroup name	P 21 3
Unit cell lengths	107.100, 107.100, 107.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.890 - 1.800
Rwork	0.190
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	2.317
Data reduction software	CrystFEL
Data scaling software	PRIME
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.890	1.930
High resolution limit [Å]	1.800	1.900
Number of reflections	38160	3121
<I/σ(I)>	4	2.1
Completeness [%]	100.0	100
Redundancy	233.7	159.9
CC(1/2)	0.938	0.639

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	BATCH MODE		291	Final concentrations: 20 mg/mL protein, 50 mM HEPES pH 7.5, 34 % (v/v) polyethylene glycol 550, 500 mM MES pH 6.5, 5 mM ZnSO4.