1K50

A V49A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-06-25
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43
Unit cell lengths	53.134, 53.134, 115.514
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.140 - 1.800
R-factor	0.211 *
Rwork	0.214
R-free	0.23900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hz6
RMSD bond length	0.006 *
RMSD bond angle	1.250 *
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.047	0.435
Total number of observations	134022 *
Number of reflections	29286 *
<I/σ(I)>	30.9	2.3
Completeness [%]	98.7 *	93.3
Redundancy	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	277	18% PEG3350, 0.2M (NH4)2SO4, 100mM Citrate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	sodium phosphate	15 (mM)	pH7.0
2	1	reservoir	PEG3350	18 (%)
3	1	reservoir	ammonium sulfate	0.2 (M)
4	1	reservoir	citrate	100 (mM)	pH4.5