title: Crystallization and preliminary X-ray investigation of recombinant human interleukin 4.
abstract: Crystals of recombinant human interleukin 4 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space-group P4(1)2(1)2 or P4(3)2(1)2; the unit cell axes are a = 92.2(1) A and c = 46.4(1) A. The crystals are stable to X-rays for at least three days and diffract beyond 2.8 A resolution. The crystals contain approximately 63% solvent, assuming there is one molecule in the asymmetric unit.
authors.affiliation: Department of Pathology, University of Alabama, Birmingham 35294.
authors.forename: W J
authors.initials: WJ
authors.lastname: Cook
authors.forename: S E
authors.initials: SE
authors.lastname: Ealick
authors.forename: P
authors.initials: P
authors.lastname: Reichert
authors.forename: G S
authors.initials: GS
authors.lastname: Hammond
authors.forename: H V
authors.initials: HV
authors.lastname: Le
authors.forename: T L
authors.initials: TL
authors.lastname: Nagabhushan
authors.forename: P P
authors.initials: PP
authors.lastname: Trotta
authors.forename: C E
authors.initials: CE
authors.lastname: Bugg
mesh_terms: D006801:Humans; D015847:Interleukin-4 / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D015847:Interleukin-4