1BSI

HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN

Experimental procedure

Temperature [K]	298
Spacegroup name	P 21 21 21
Unit cell lengths	52.910, 68.900, 131.770
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.000
R-factor	0.184
Rwork	0.184
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.450
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.000	2.000 *
Rmerge	0.075	0.184 *
Total number of observations	166575 *
Number of reflections	33646
Completeness [%]	95.4
Redundancy	5.0 *	2.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		pH 7.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MPD	60 (%)
2	1	reservoir	cacodylate	100 (mM)	pH7.5
3	1	drop	protein	2 (mg/ml)