Crystallization and initial crystal characterization of the C-terminal phosphoglycerate mutase homology domain of Sts-1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Holly KleinmanNicolas Nassar

Abstract

Sts-1 is a multidomain protein that plays an important role in T-cell signaling. Sts-1 contains a ubiquitin-association (UBA) domain at the N-terminus, followed by an Src homology-3 (SH3) domain and a C-terminal domain that shares sequence homology to phosphoglycerate mutases (PGMs). The C-terminal domain of Sts-1, Sts-1(PGM), crystallizes in space group C2 with two different crystal forms. The first crystal form contains two or three Sts-1PGM molecules in the asymmetric unit and diffracts to 1.82 A resolution, with unit-cell parameters a = 116.2, b = 74.3, c = 100.1 A, alpha = gamma = 90, beta = 101.5 degrees. The second crystal form contains four or six Sts-1(PGM) molecules in the asymmetric unit, with unit-cell parameters a = 214.9, b = 75.1, c = 116.4 A, alpha = gamma = 90, beta = 111.6 degrees. Greater than 95% complete native and SeMet data sets have been collected and structure determination using the multiple anomalous dispersion (MAD) technique is ongoing.

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Citations

Jan 1, 1997·Comptes rendus de l'Académie des sciences. Série III, Sciences de la vie·P RavelD Toullec
Jun 3, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Jean JakoncicNicolas Nassar
Aug 7, 2007·Molecular Cell·Anatoly MikhailikNick Carpino
Mar 18, 2008·IUBMB Life·Alexander Y Tsygankov

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