1HMR

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, 55.420, 71.310
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 1.400
R-factor	0.132
Rwork	0.132
RMSD bond length	0.019
RMSD bond angle	2.540
Phasing software	X-PLOR
Refinement software	SHELXL

Data quality characteristics

	Overall
Low resolution limit [Å]	35.800 *
High resolution limit [Å]	1.360 *
Rmerge	0.100 *
Total number of observations	92367 *
Number of reflections	26005 *
Completeness [%]	83.4 *

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	38 (%)
3	1	reservoir	piperazine-N-N'-bis[2-ethanesulfonic acid]	20 (mM)