6MC0

Crystal Structure of Ribose-5-phosphate Isomerase from Legionella pneumophila with Bound Substrate Ribose-5-Phosphate and Product Ribulose-5-Phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2018-08-23
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	103.290, 67.560, 73.320
Unit cell angles	90.00, 118.82, 90.00

Refinement procedure

Resolution	45.247 - 2.000
R-factor	0.1576
Rwork	0.154
R-free	0.20280
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6eep
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.14_3228))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	45.247	45.247	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.064	0.022	0.449
Rmeas	0.074	0.025	0.551
Total number of observations	121457
Number of reflections	29874	356	2202
<I/σ(I)>	15.57	57.92	2.22
Completeness [%]	99.3	97.5	99.6
Redundancy	4.066	4.303	2.592
CC(1/2)	0.999	1.000	0.793

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	LepnA.00944.a.B1.PS38423 at 22.85 mg/ml was mixed 1:1 with MCSG1(B8): 25.5% (w/v) PEG-4,000, 15% (v/v) Glycerol, 0.085 M Tris Base / Hydrochloric, 0.17 M Sodium Acetate, pH = 8.5.Crystals from tray 300294b8 were then soaked overnight mixed 1:1 with MCSG1(B8) condition suplemented with 5 mM ribulose-5-phosphate. Tray: 300294b8. Puck: kbr1-2