3LL4

Structure of the H13A mutant of Ykr043C in complex with fructose-1,6-bisphosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2009-12-14
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.54178
Spacegroup name	P 21 21 21
Unit cell lengths	83.620, 84.022, 101.568
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.390 - 2.490
R-factor	0.22468
Rwork	0.223
R-free	0.26630
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3F3K molecule A
RMSD bond length	0.015
RMSD bond angle	1.554
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.390	2.540
High resolution limit [Å]	2.500	2.500
Rmerge	0.104	0.484
Number of reflections	25181
<I/σ(I)>	21.28	4.7
Completeness [%]	98.0	89.1
Redundancy	5	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	294	resevoir of 0.1M Sodium Hepes ph7.5, 10% isopropanol and 20% PEG4K. 0.03 mg/ml trypsin was added to the protein prior to crystallization setup. Crystals were washed in well solution, then soaked in well solution plus 12% Glycerol and 0.1M fructose 1,6 bis-phosphate at room temperature for 10 minutes prior to flash-freezing in liquid N2, VAPOR DIFFUSION, HANGING DROP, temperature 294K