Journal article
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, Vol.62(Pt 3), pp.218-220
03/2006
DOI: 10.1107/S1744309106003320
PMCID: PMC2197191
PMID: 16511305
Abstract
The C-terminal domain of the signaling protein Sts-1 has been expressed in bacteria, purified and crystallized and diffraction data sets have been collected from two crystal forms.
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
C
2 with two different crystal forms. The first crystal form contains two or three Sts-1
PGM
molecules in the asymmetric unit and diffracts to 1.82 Å resolution, with unit-cell parameters
a
= 116.2,
b
= 74.3,
c
= 100.1 Å, α = γ = 90, β = 101.5°. 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 Å, α = γ = 90, β = 111.6°. Greater than 95% complete native and SeMet data sets have been collected and structure determination using the multiple anomalous dispersion (MAD) technique is ongoing.
Details
- Title: Subtitle
- Crystallization and initial crystal characterization of the C-terminal phosphoglycerate mutase homology domain of Sts-1
- Creators
- Holly Kleinman - Department of Physiology and Biophysics, Basic Sciences Tower, Stony Brook University, Stony Brook, NY 11794-8661Bradley Ford - Department of Physiology and Biophysics, Basic Sciences Tower, Stony Brook University, Stony Brook, NY 11794-8661James Keller - Department of Molecular Genetics and Microbiology, Life Sciences Building, Stony Brook University, Stony Brook, NY 11794-5222Nick Carpino - Department of Molecular Genetics and Microbiology, Life Sciences Building, Stony Brook University, Stony Brook, NY 11794-5222Nicolas Nassar - Department of Physiology and Biophysics, Basic Sciences Tower, Stony Brook University, Stony Brook, NY 11794-8661
- Resource Type
- Journal article
- Publication Details
- Acta crystallographica. Section F, Structural biology and crystallization communications, Vol.62(Pt 3), pp.218-220
- DOI
- 10.1107/S1744309106003320
- PMID
- 16511305
- PMCID
- PMC2197191
- NLM abbreviation
- Acta Crystallogr Sect F Struct Biol Cryst Commun
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- Publisher
- International Union of Crystallography
- Alternative title
- PGM homology domain of Sts-1
- Language
- English
- Date published
- 03/2006
- Academic Unit
- Pathology
- Record Identifier
- 9984047999502771
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