3B35

Crystal structure of the M180A mutant of the aminopeptidase from Vibrio proteolyticus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Wavelength(s)	0.90010
Spacegroup name	P 61 2 2
Unit cell lengths	109.148, 109.148, 90.990
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	41.000 - 1.100
R-factor	0.15
Rwork	0.149
R-free	0.16600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1amp
RMSD bond length	0.012
RMSD bond angle	1.533
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.000
High resolution limit [Å]	1.100	1.100
Rmerge	0.059
Number of reflections	122065
<I/σ(I)>		2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	HEPES, KSCN, NaCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K