6APE

Crystal Structure of Bifunctional protein FolD from Helicobacter pylori

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	2017-06-23
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 2 2 21
Unit cell lengths	69.880, 109.040, 83.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	33.222 - 1.450
R-factor	0.1675
Rwork	0.167
R-free	0.18240
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3p2o
RMSD bond length	0.006
RMSD bond angle	0.794
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.12rc2_2821)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	33.222	33.222	1.490
High resolution limit [Å]	1.450	6.480	1.450
Rmerge	0.035	0.025	0.421
Rmeas	0.037	0.028	0.454
Total number of observations	409285
Number of reflections	56895	700	4133
<I/σ(I)>	28.34	61.72	4.19
Completeness [%]	99.9	97	100
Redundancy	7.194	6.133	7.178
CC(1/2)	1.000	0.999	0.935

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Tray 291037 Morpheus A3: 10% w/v PEG 4000, 20% v/v glycerol 0.03 M of each divalent cation (0.3 M magnesium chloride, 0.3 M calcium chloride) 0.1 M MES/imidazole pH 6.5 : cryo: direct: HepyC.00934.a.B1 PS38251 at 20 mg/ml, puck mxk4-8