5MJ6

Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2014-12-06
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	0.976
Spacegroup name	P 21 21 21
Unit cell lengths	112.240, 143.170, 148.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.805 - 2.530
R-factor	0.1766
Rwork	0.174
R-free	0.22920
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2yd0
RMSD bond length	0.010
RMSD bond angle	1.378
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHASER
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.805	2.600
High resolution limit [Å]	2.530	2.530
Rmerge	0.199
Number of reflections	80735
<I/σ(I)>	0.812	1.6
Completeness [%]	100.0	100
Redundancy	13.2	13.1
CC(1/2)	0.997	0.451

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	18.8% (w/v) PEG of mean MW 20000, 37.6% (v/v) PEG monomethyl ether of mean MW 500, 50.2 mM Bicine, 43.8 mM Trizma base (pH of buffer mixture: 8.5) and 0.282 M each of the following halogens: Sodium fluoride, Sodium bromide and Sodium iodide