1HEZ

Structure of P. magnus protein L bound to a human IgM Fab.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1999-10-15
Detector	MAR scanner 345 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	55.185, 87.335, 210.538
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.215
Rwork	0.215
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dee
RMSD bond length	0.007
RMSD bond angle	1.423
Data reduction software	HKL
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.780
High resolution limit [Å]	2.600 *	2.600 *
Rmerge	0.116 *	0.486 *
Number of reflections	26811
<I/σ(I)>	12.7	2.9
Completeness [%]	95.2	93.7 *
Redundancy	4.66	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.5		used seeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mPEG5000	13-16 (%(w/w))
2	1	reservoir	imidazole malate	100 (mM)
3	1	drop	protein	5 (mg/ml)