8D1X

Crystal Structure of aminopeptidase A from Neisseria gonorrhoeae

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	2016-08-04
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	96.610, 93.250, 179.470
Unit cell angles	90.00, 101.32, 90.00

Refinement procedure

Resolution	48.170 - 2.800
R-factor	0.1706
Rwork	0.170
R-free	0.20250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3jru as per Morda
RMSD bond length	0.004
RMSD bond angle	0.627
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (1.20.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.870
High resolution limit [Å]	2.800	12.520	2.800
Rmerge	0.122	0.055	0.551
Rmeas	0.139	0.064	0.630
Number of reflections	77236	897	5667
<I/σ(I)>	9.61	20.42	2.58
Completeness [%]	99.9	96.1	100
Redundancy	4.263	3.751	4.302
CC(1/2)	0.992	0.993	0.827

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	287	Molecular Dimensions / Calibre Morpheus screen, condition G6: 10% w/v PEG 8000, 20% v/v ethylene glycol: 20mM of each sodium formate, ammonium acetate, trisodium citrate, sodium potassium L-tartrate, sodium oxamate, 100mM MOPS/HEPES-Na pH 7.5: NegoA.00799.a.B1.PW37906 at 19mg/ml + 2mM MnCl2: tray 273710 g6: cryo: direct: puck ifb3-2.