1KRF

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	2000-03-20
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	0.199 *
Rwork	0.199
R-free	0.23640
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1kkt
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	2.200
High resolution limit [Å]	2.140	2.140
Rmerge	0.074	0.376 *
Total number of observations	225764 *
Number of reflections	57692
<I/σ(I)>	20.1
Completeness [%]	98.7	89.3
Redundancy	3.91

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5 *	293	PEG 6000, potassium phosphate, pH 4.60, 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