1HY5

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF YOPE-YERSINIA PESTIS GAP EFFECTOR PROTEIN.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-10-05
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	62.692, 71.978, 62.684
Unit cell angles	90.00, 113.06, 90.00

Refinement procedure

Resolution	100.000 - 2.250
R-factor	0.1761
Rwork	0.197
R-free	0.23830
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.330
High resolution limit [Å]	2.250	2.250
Rmerge	0.060 *	0.221 *
Number of reflections	22062 *
<I/σ(I)>	16	4
Completeness [%]	98.9 *	96.2
Redundancy	2.3 *	1.8 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7 *	300	Ammonium sulphate, bicine, potassium nitrate, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 300K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	1.2-1.6 (M)
2	1	reservoir	HEPES	100 (mM)	pH7.0(or Bicine pH9.0)
3	1	reservoir	potassium nitrate	100-200 (mM)