8A5R

Crystal structure of light-activated DNA-binding protein EL222 from Erythrobacter litoralis crystallized and measured in dark.

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	LIQUID ANODE
Source details	Excillum MetalJet D2 70 kV
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-02-20
Detector	Bruker PHOTON II
Wavelength(s)	1.3418
Spacegroup name	P 21 21 21
Unit cell lengths	43.810, 51.961, 81.063
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.975 - 1.850
R-factor	0.1607
Rwork	0.160
R-free	0.21528
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3p7n
RMSD bond length	0.011
RMSD bond angle	1.727
Data reduction software	PROTEUM
Data scaling software	SADABS
Phasing software	MOLREP (11.7.02)
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.975	1.890
High resolution limit [Å]	1.850	1.850
Rmerge	0.070	0.437
Rmeas	0.078	0.567
Rpim	0.035	0.355
Number of reflections	15648	680
<I/σ(I)>	13.2	2.5
Completeness [%]	95.6	69.6
Redundancy	4.6	2.2
CC(1/2)	0.998	0.773

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	291.15	21% (w/v) PEG 8000, 0.22 M MgCl2, 0.11 M MES pH 6.5