1L2H

Crystal structure of Interleukin 1-beta F42W/W120F mutant

Summary for 1L2H

• Entry DOI: 10.2210/pdb1l2h/pdb
• Related: 9ilb
• Descriptor: Interleukin 1-beta (2 entities in total)
• Functional Keywords: interleukin-1 beta, beta-trefoil, f42w/w120f double mutant, protein folding, mad phasing, hemihedral twinning, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P01584
• Total number of polymer chains: 1
• Total formula weight: 17395.83

Authors

Rudolph, M.G.,Kelker, M.S.,Schneider, T.R.,Yeates, T.O.,Oseroff, V.,Heidary, D.K.,Jennings, P.A.,Wilson, I.A. (deposition date: 2002-02-21, release date: 2003-02-04, Last modification date: 2024-02-14)

Primary citation

Rudolph, M.G.,Kelker, M.S.,Schneider, T.R.,Yeates, T.O.,Oseroff, V.,Heidary, D.K.,Jennings, P.A.,Wilson, I.A.
Use of multiple anomalous dispersion to phase highly merohedrally twinned crystals of interleukin-1beta.
Acta Crystallogr.,Sect.D, 59:290-298, 2003

PubMed Abstract: The crystal structure at 1.54 A resolution of a double mutant of interleukin-1beta (F42W/W120F), a cytokine secreted by macrophages, was determined by multiple-wavelength anomalous dispersion (MAD) using data from highly twinned selenomethionine-modified crystals. The space group is P4(3), with unit-cell parameters a = b = 53.9, c = 77.4 A. Self-rotation function analysis and various intensity statistics revealed the presence of merohedral twinning in crystals of both the native (twinning fraction alpha approximately 0.35) and SeMet (alpha approximately 0.40) forms. Structure determination and refinement are discussed with emphasis on the possible reasons for successful phasing using untreated twinned MAD data.

PubMed: 12554939
DOI: 10.1107/S0907444902021704

Experimental method

X-RAY DIFFRACTION (1.54 Å)