1KKT

Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	AREA DETECTOR
Collection date	2000-02-26
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	56.487, 110.997, 86.235
Unit cell angles	90.00, 99.17, 90.00

Refinement procedure

Resolution	50.000 - 2.200
R-factor	0.193 *
Rwork	0.193
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENTRIES 1DL2 and 1FM1
RMSD bond length	0.006 *
RMSD bond angle	1.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.250
High resolution limit [Å]	2.200	2.200
Rmerge	0.069	0.243 *
Total number of observations	174227 *
Number of reflections	49836 *
<I/σ(I)>	16.3
Completeness [%]	92.6	60.1
Redundancy	3.49

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5 *	293	PEG 6000, potassium phosphate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	sodium acetate	10 (mM)	pH5.0
3	1	reservoir	PEG6000	17-22 (%)
4	1	reservoir	potassium phosphate	50 (mM)	pH4.6