6OAD

2.05 Angstrom Resolution Crystal Structure of Aminopeptidase B from Escherichia coli str. K-12 substr. MG1655.

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	2019-02-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	150.667, 114.761, 161.171
Unit cell angles	90.00, 92.02, 90.00

Refinement procedure

Resolution	29.880 - 2.050
R-factor	0.17398
Rwork	0.172
R-free	0.21473
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ij3
RMSD bond length	0.006
RMSD bond angle	1.473
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MoRDa
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.090
High resolution limit [Å]	2.050	2.050
Rmerge	0.098	0.791
Rmeas	0.112	0.905
Rpim	0.054	0.437
Number of reflections	338775	16506
<I/σ(I)>	11.9	1.9
Completeness [%]	98.8	96.4
Redundancy	4.1	4.1
CC(1/2)		0.761

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	292	Protein: 6.0 mg/ml, 0.01M Tris pH 8.3; Screen: PEGs II (H8), 0.2M Calcium acetate, 0.1M HEPES pH 7.5, 10% (w/v) PEG 8000. Cryo: reservoir + 20% Ethylene glycol.