4C8E

IspF (Burkholderia cenocepacia) 2CMP complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-04-05
Detector	RIGAKU RAXIS IV PLUS PLUS
Spacegroup name	C 1 2 1
Unit cell lengths	97.849, 89.316, 72.981
Unit cell angles	90.00, 104.18, 90.00

Refinement procedure

Resolution	70.760 - 1.900
R-factor	0.20601
Rwork	0.204
R-free	0.25064
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3f0g
RMSD bond length	0.011
RMSD bond angle	1.526
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.320	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.140	0.320
Number of reflections	47918
<I/σ(I)>	6.2	3.1
Completeness [%]	99.9	100
Redundancy	3.4	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	293	PROTEIN WAS CRYSTALLISED BY HANGING-DROP VAPOUR DIFFUSION. BCISPF SAMPLE IN 100 MM NACL, 2MM MGCL2, 100 MM TRIS-HCL, PH 7.5; WAS CONCENTRATED TO 5 MG/ML, AND HAD CMP ADDED (20 MM CONCENTRATION IN SAMPLE). CRYSTALS WERE OBTAINED BY MIXING 2 MICROLITRES OF SAMPLE WITH 2 MICROLITRES RESERVOIR AT 20 DEGREES C. RESERVOIR SOLUTION: 25% W/V PEG 3350, 2.2M (NH4)2SO4, 0.1 M SODIUM FORMATE, PH 5.0, 1% V/V DIOXANE. CRYO: 20% GLYCEROL.