1CP3

CRYSTAL STRUCTURE OF THE COMPLEX OF APOPAIN WITH THE TETRAPEPTIDE INHIBITOR ACE-DVAD-FMC

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1996-02
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	50.900, 69.100, 93.800
Unit cell angles	90.00, 101.20, 90.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.188
Rwork	0.188
R-free	0.28400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	A HOMOLOGY MODEL WAS USED
RMSD bond length	0.013
RMSD bond angle	25.680 *
Data reduction software	MARXDS
Data scaling software	MARSCALE
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.500
High resolution limit [Å]	2.300	2.300
Rmerge	0.069	0.237
Number of reflections	24128	5092 *
<I/σ(I)>	12.9	3.7
Completeness [%]	83.7	78.6
Redundancy	1.6	1.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.4	4 *	HANGING DROP, RESERVOIR: 5% PEG8000, 0.05 M MAGNESIUM ACETATE, 0.09 M SODIUM CACODYLATE, 0.08 M SODIUM SULFATE, PH 6.4, 4 DEG. CELSIUS, vapor diffusion - hanging drop, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.3 (mg/ml)
2	1	reservoir	PEG8000	5 (%(w/v))
3	1	reservoir	magnesium acetate	50 (mM)
4	1	reservoir	sodium cacodylate	90 (mM)
5	1	reservoir	sodium sulphate	80 (mM)