2MPR

MALTOPORIN FROM SALMONELLA TYPHIMURIUM

Experimental procedure

Source type	ROTATING ANODE
Source details	MACSCIENCE M18X
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1995-09-04
Detector	SIEMENS-NICOLET X100
Spacegroup name	C 2 2 21
Unit cell lengths	124.500, 211.800, 184.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.400
R-factor	0.191
Rwork	0.191
R-free	0.22200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mpr
RMSD bond length	0.010
RMSD bond angle	27.400 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	AMoRE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.480
High resolution limit [Å]	2.400	2.400
Rmerge	0.070	0.350 *
Total number of observations	278202 *
Number of reflections	90607
<I/σ(I)>	12	4.3
Completeness [%]	88.0 *	62 *
Redundancy	3.1	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		18 *	MALTOPORIN WAS CRYSTALLIZED BY HANGING-DROP METHOD. DROP: 5-8 MG/ML PROTEIN, 0.3% C8E4, 0.8% C6DAO, 1 MM CACL2, 1MM MGCL2, 14-18% PEG 1500, 0.02% NAN3 RESERVOIR: 28-32% PEG 1500, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5-8 (mg/ml)
2	1	drop	n-octyltetraoxyethylene	0.3 (%)
3	1	drop	n-hexyldimethylaminoxide	0.8 (%)
4	1	drop		1 (mM)
5	1	drop		1 (mM)
6	1	drop	PEG1500	14-18 (%)
7	1	drop		0.02 (%)
8	1	reservoir	PEG1500	28-32 (%)