1MHH

Structure of P. magnus protein L mutant bound to a mouse Fab

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-02-18
Detector	ADSC QUANTUM 4
Wavelength(s)	0.934
Spacegroup name	P 21 21 21
Unit cell lengths	78.486, 100.957, 149.147
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
Rwork	0.197
R-free	0.24700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.160
High resolution limit [Å]	2.100	2.100
Rmerge	0.067 *	0.417 *
Number of reflections	69723
<I/σ(I)>	26.6	3.5
Completeness [%]	97.6	85
Redundancy	6.77	5.86

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	10%(wt/wt) MPEG 5K, 100mM sodium acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1	VAPOR DIFFUSION, SITTING DROP	4.5	293	10%(wt/wt) MPEG 5K, 100mM sodium acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Fab	6 (mg/ml)
2	1	drop	PpL	16 (mg/ml)
3	1	reservoir	MPEG5000	10 (%(w/w))
4	1	reservoir	sodium acetate	100 (mM)	pH4.5