3CXK
1.7 A Crystal structure of methionine-R-sulfoxide reductase from Burkholderia pseudomallei: crystallization in a microfluidic crystal card.
Summary for 3CXK
| Entry DOI | 10.2210/pdb3cxk/pdb |
| Related | 3CEZ |
| Descriptor | Methionine-R-sulfoxide reductase, ZINC ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | structural genomics, burkholderia, msrb, oxidoreductase, microfluidic labcard, psi-2, protein structure initiative, accelerated technologies center for gene to 3d structure, atcg3d, seattle structural genomics center for infectious disease, ssgcid |
| Biological source | Burkholderia pseudomallei strain |
| Total number of polymer chains | 2 |
| Total formula weight | 37247.97 |
| Authors | Lovell, S.,Gerdts, C.,Staker, B.,Craigen, D.,Stewart, L.,Accelerated Technologies Center for Gene to 3D Structure (ATCG3D),Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2008-04-24, release date: 2008-05-27, Last modification date: 2023-08-30) |
| Primary citation | Gerdts, C.J.,Elliott, M.,Lovell, S.,Mixon, M.B.,Napuli, A.J.,Staker, B.L.,Nollert, P.,Stewart, L. The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS). Acta Crystallogr.,Sect.D, 64:1116-1122, 2008 Cited by PubMed Abstract: The Microcapillary Protein Crystallization System (MPCS) embodies a new semi-automated plug-based crystallization technology which enables nanolitre-volume screening of crystallization conditions in a plasticware format that allows crystals to be easily removed for traditional cryoprotection and X-ray diffraction data collection. Protein crystals grown in these plastic devices can be directly subjected to in situ X-ray diffraction studies. The MPCS integrates the formulation of crystallization cocktails with the preparation of the crystallization experiments. Within microfluidic Teflon tubing or the microfluidic circuitry of a plastic CrystalCard, approximately 10-20 nl volume droplets are generated, each representing a microbatch-style crystallization experiment with a different chemical composition. The entire protein sample is utilized in crystallization experiments. Sparse-matrix screening and chemical gradient screening can be combined in one comprehensive ;hybrid' crystallization trial. The technology lends itself well to optimization by high-granularity gradient screening using optimization reagents such as precipitation agents, ligands or cryoprotectants. PubMed: 19020349DOI: 10.1107/S0907444908028060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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