1QMY

FMDV LEADER PROTEASE (LBSHORT-C51A-C133S)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	1999-04-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	46.064, 110.751, 56.966
Unit cell angles	90.00, 98.75, 90.00

Refinement procedure

Resolution	19.740 - 1.900
R-factor	0.189 *
Rwork	0.190
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.015
RMSD bond angle	25.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS (0.9)
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.032 *	0.215 *
Number of reflections	42246
<I/σ(I)>	16.5	4.2
Completeness [%]	95.0	93
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		20% PEG 8000, 0.2 M MG ACETATE, 0.1 M NA CACODYLATE, PH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	20 (%(w/v))
2	1	reservoir	magnesium acetate	0.2 (M)
3	1	reservoir	sodium cacodylate	0.1 (M)