6VJ2

3.10 Angstrom Resolution Crystal Structure of Foldase Protein (PrsA) from Lactococcus lactis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2018-08-16
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	81.513, 117.609, 149.310
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.400 - 3.100
R-factor	0.2364
Rwork	0.234
R-free	0.28970
Structure solution method	SAD
RMSD bond length	0.004
RMSD bond angle	1.241
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.150
High resolution limit [Å]	3.100	3.100
Rmerge	0.122	0.776
Rmeas	0.137	0.867
Rpim	0.061	0.381
Number of reflections	26817	1306
<I/σ(I)>	13.7	2.1
Completeness [%]	99.9	100
Redundancy	4.9	5
CC(1/2)		0.787

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	292	Protein: 6.4 mg/ml, 0.01M Tris HCl (pH 8.3); Reservoir (PEGs II screen, B6): 0.1M HEPES (pH 7.5), 20% (w/v) PEG 1500