4LA0

X-ray study of human serum albumin complexed with bicalutamide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-01-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 1
Unit cell lengths	56.444, 59.568, 95.957
Unit cell angles	73.22, 83.93, 74.17

Refinement procedure

Resolution	29.861 - 2.400
R-factor	0.2018
Rwork	0.199
R-free	0.25400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.011
RMSD bond angle	1.445
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MERLOT
Refinement software	PHENIX (1.8.2_1309)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.000	30.000	2.490
High resolution limit [Å]	2.400	5.160	2.400
Rmerge	0.068	0.033	0.454
Number of reflections	41969
<I/σ(I)>	10.6
Completeness [%]	93.3	94.2	83.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	PEG 3350, POTASSIUM PHOSPHATE, Crystals of the complexes were obtained by standard vapor equilibration methods with conditions optimized by screens varying protein concentration, pH, drug molar ratios, centered on the original crystallization hit using protocols described previously for the monoclinic [Carter, et al., Eur. J. Biochemistry (1994) 226: 1049-1052] and triclinic [Sugo, et al., Protein Eng (1999) 12: 439-446] crystal forms., pH 7.5, vapor diffusion, SITTING DROP, temperature 293K