6OV8

2.6 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	2019-04-12
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9787
Spacegroup name	P 21 21 21
Unit cell lengths	114.857, 148.190, 165.010
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.760 - 2.610
R-factor	0.18411
Rwork	0.181
R-free	0.23760
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6oad
RMSD bond length	0.003
RMSD bond angle	1.042
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0238)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.640
High resolution limit [Å]	2.600	2.600
Rmerge	0.136	0.790
Rmeas	0.149	0.861
Rpim	0.059	0.341
Number of reflections	85965	4231
<I/σ(I)>	14.4	2.5
Completeness [%]	100.0	100
Redundancy	6.2	6.3
CC(1/2)		0.837

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	292	Protein: 8.2 mg/ml, 0.5M Sodium chloride, 0.01M Tris pH 8.3, 1mM Zn, 1mM Mn Screen: Classics II (F10), 0.2M Sodium chloride, 0.1M BIS-TRIS pH 5.5, 25% (w/v) PEG 3350