1HZ6

CRYSTAL STRUCTURES OF THE B1 DOMAIN OF PROTEIN L FROM PEPTOSTREPTOCOCCUS MAGNUS WITH A TYROSINE TO TRYPTOPHAN SUBSTITUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-10-05
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	51.611, 54.020, 95.069
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 1.700
R-factor	0.193
Rwork	0.193
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	C3 DOMAIN OF PROTEIN L (UNPUBLISHED: T. WAN AND B. SUTTON)
RMSD bond length	0.006
RMSD bond angle	25.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.710
High resolution limit [Å]	1.700	1.690
Rmerge	0.074	0.273
Number of reflections	28825
<I/σ(I)>	17	6.8
Completeness [%]	96.3	95.1
Redundancy	4.94	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	277	30%PEG 8000, 0.2M Ammonium Sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	(%)
2	1	reservoir	ammonium sulfate	(M)
3	1	reservoir	PEG400	(%)	cryoprotectant