6Q92

Crystal structure of human Arginase-1 at pH 7.0 in complex with ABH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-09-06
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.966
Spacegroup name	P 3
Unit cell lengths	90.380, 90.380, 69.254
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	39.140 - 1.500
R-factor	0.13544
Rwork	0.135
R-free	0.14721
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2aeb
RMSD bond length	0.007
RMSD bond angle	1.306
Data reduction software	MOSFLM (7.2.0)
Data scaling software	Aimless (0.7.1)
Phasing software	MOLREP (11.6.02)
Refinement software	REFMAC (5.8.0218)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.140	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.097	0.608
Rmeas	0.122	0.796
Rpim	0.074	0.508
Number of reflections	99464	4790
<I/σ(I)>	6.9	1.8
Completeness [%]	98.2	96.4
Redundancy	2.4	2.1
CC(1/2)	0.987	0.293

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4	293	Crystals were generated from 22 % PEG 1500, 0.2 M MIB buffer pH 4.0 (sodium malonate, imidazole and boric acid in a 2:3:3 molar ratio). Crystals were equilibrated to soaking solution (22 % PEG 1500, 0.2 M MMT buffer pH 7.0 (DL-malic acid, MES, Tris base in a 1:2:2 molar ratio). Subsequently, crystals were gradually soaked for 13 days in soaking solution containing 15 mM ABH.