1JML

Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	2000-12-08
Detector	RIGAKU RAXIS IV
Spacegroup name	C 2 2 21
Unit cell lengths	46.762, 76.744, 59.797
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	23.590 - 1.900
R-factor	0.193 *
Rwork	0.193
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hz5
RMSD bond length	0.008
RMSD bond angle	1.400
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.940
High resolution limit [Å]	1.900	1.900
Rmerge	0.064	0.170
Total number of observations	39485 *
Number of reflections	8777
<I/σ(I)>	16.6	7.8
Completeness [%]	99.7	99.3
Redundancy	4.5	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	175mM Zinc Acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		175 (mM)
2	1	reservoir	cacodylate	50 (mM)