1O7D

The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Detector	ADSC CCD
Spacegroup name	P 61 2 2
Unit cell lengths	117.880, 117.880, 582.040
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.700
R-factor	0.257
Rwork	0.257
R-free	0.28900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hty
RMSD bond length	0.010
RMSD bond angle	24.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.760
High resolution limit [Å]	2.700	2.700
Rmerge	0.090	0.540
Number of reflections	60071
<I/σ(I)>	15.9	2.1
Completeness [%]	89.4 *	77.7 *
Redundancy	3	3.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5		PROTEIN 9 MG/ML IN 20 MM TRIS-CL, PH 7.5, 150 MM NACL MIXED 1:1 WITH 100 MM TRIS-CL, PH 7.5, 50 % SAT. (NH4)2SO4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	9 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH7.5
3	1	drop		150 (mM)
4	1	reservoir	ammonium sulfate	50 (%sat)
5	1	reservoir	Tris-HCl	100 (mM)	pH7.5