3N25

The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-07-18
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.54
Spacegroup name	P 1
Unit cell lengths	82.373, 108.747, 144.256
Unit cell angles	95.18, 93.38, 112.23

Refinement procedure

Resolution	36.590 - 2.410
R-factor	0.207
Rwork	0.204
R-free	0.26800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.125
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.490
High resolution limit [Å]	2.400	5.170	2.400
Rmerge	0.123	0.058	0.504
Number of reflections	146924
<I/σ(I)>	8.9
Completeness [%]	83.6	96	78.8
Redundancy	3.5	3.7	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	hanging drop vapor diffusion	5.5	298	60 mM Succinate (pH 5.5), 5.8 mM sodium pyruvate, 2.4 mM MnCl2, 450 mM KCl, 444 mM Proline and a range of 18 to 20% PEG 8000., hanging drop vapor diffusion, temperature 298K