1HMS

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

Experimental procedure

Spacegroup name	P 21 21 21
Unit cell lengths	34.650, 55.450, 71.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.400
R-factor	0.121
Rwork	0.121
RMSD bond length	0.019
RMSD bond angle	2.660
Phasing software	X-PLOR
Refinement software	SHELXL

Data quality characteristics

	Overall
Low resolution limit [Å]	31.200 *
High resolution limit [Å]	1.240 *
Rmerge	0.075 *
Total number of observations	78811 *
Number of reflections	32605 *
Completeness [%]	80.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.1 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25-30 (mg/ml)
2	1	reservoir	PEG4000	28-30 (%)
3	1	reservoir	piperazine-N-N'-bis[2-ethanesulfonic acid]	20 (mM)