4ND2

Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor analog (3-acetylpyridine adenine dinucleotide)

Replaces:  2EWD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2004-07-03
Detector	MARRESEARCH
Wavelength(s)	0.9998
Spacegroup name	P 32 2 1
Unit cell lengths	95.830, 95.830, 185.640
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.610 - 2.000
R-factor	0.19299
Rwork	0.191
R-free	0.20788
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1t2d
RMSD bond length	0.004
RMSD bond angle	0.925
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.054	0.186
Number of reflections	67287
Completeness [%]	99.8	97.7
Redundancy	10.7	8.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	277	The protein was incubated with 1 mM pyruvate and 100 uM APAD+ for 1 hour on ice prior to crystallization. Reservoir solution was 1.45-1.65 M ammonium sulfate in 0.1 M sodium cacodylate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K