1IWO

Crystal structure of the SR Ca2+-ATPase in the absence of Ca2+

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL44XU
Synchrotron site	SPring-8
Beamline	BL44XU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-12-10
Detector	MACSCIENCE
Wavelength(s)	0.900
Spacegroup name	P 41
Unit cell lengths	71.739, 71.739, 590.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 3.100
R-factor	0.237
Rwork	0.237
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	cytoplasmic domains of 1EUL
RMSD bond length	0.009
RMSD bond angle	22.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.180
High resolution limit [Å]	3.100	3.100
Rmerge	0.092	0.437
Number of reflections	51314
<I/σ(I)>	21.3	3
Completeness [%]	97.9	97.4
Redundancy	7.1 *	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	6.1	283	PEG 400, MES, EGTA, glycerol, magnesium chloride, pH 6.1, MICRODIALYSIS, temperature 283K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	0.020 (mM)
10	1	2	butylhydroxytoluene	0.002 (mg/ml)
11	1	2	dithiothreitol	0.2 (mM)
12	1	2	EGTA	0.1 (mM)
13	1	2	MES	20 (mM)	pH6.1
2	1	1		2. (mg/ml)
3	1	1	Ca2+	1 (mM)
4	1	1	thapsigargin	0.030 (mM)
5	1	1	EGTA	3 (mM)
6	1	2	glycerol	2.75 (M)
7	1	2	PEG400	4 (%)
8	1	2		3 (mM)
9	1	2		2.5 (mM)