1E8A

The three-dimensional structure of human S100A12

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	120
Spacegroup name	H 3
Unit cell lengths	99.600, 99.600, 64.200
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.000 - 1.950
R-factor	0.178 *
Rwork	0.180
R-free	0.22000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mho
RMSD bond length	0.018
RMSD bond angle	1.740
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.086	0.258 *
Number of reflections	17174	1721 *
<I/σ(I)>	10.6	2.68
Completeness [%]	99.3	99.1
Redundancy	2.8	1.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5		20-25% PEG 5K MONOMETHYL ETHER, 0.2M CALCIUM CHLORIDE, 0.1M SODIUM CACODILATE, HANGING DROPS, pH 6.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.0-8.0 (mg/ml)
2	1	reservoir	sodium cacodylate	0.1 (M)	pH6.5
3	1	reservoir		0.2 (M)
4	1	reservoir	PEG5000 MME	20-25 (%)