Nanovolume optimization of protein crystal growth using the microcapillary protein crystallization system

Gerdts, C.J.; Stahl, G.L.; Napuli, A.; Staker, B.; Abendroth, J.; Edwards, T.E.; Myler, P.; Van Voorhis, W.; Nollert, P.; Stewart, L.J.

doi:10.1107/S0021889810027378

Figure 3
Pictures of crystals in plugs generated from MPCS optimizations that led to high-quality data sets (2.5 Å or better) and/or novel structures. Corresponding ribbon structures are included below the pictures of the plugs (for data collection and refinement statistics, see Table 2

). All scale bars = 200 µm. (a) Enoyl-CoA hydratase from Mycobacterium tuberculosis (1.8 Å; PDB code 3h81); (b) aldehyde dehydrogenase from Bartonella henselae (2.1 Å; PDB code 3i44; deposited structure for PDB code 3i44 came from a sitting-drop optimization at 2.0 Å resolution; the 2.1 Å-resolution data set was generated from a crystal optimized using the MPCS); (c) methionine-R-sulfoxide reductase from Burkholderia pseudomallei (1.7 Å; PDB code 3cxk); (d) methylisocitrate lyase from Brucella melitensis (2.9 Å; PDB code 3eoo); (e) dihydrofolate reductase/thymidylate synthase from Babesia bovis (2.5 Å; PDB code 3i3r); (f) tRNA guanine-n1-methyltransferase from Bartonella henselae (2.5 Å; PDB code 3ief); (g) A picture of the commercial version of the MPCS Plug Maker. Left: The touch screen user interface and live image of the CrystalCard. Right: Instrument stage that holds the CrystalCard and crystallization samples.

JOURNAL OF
APPLIED
CRYSTALLOGRAPHY

ISSN: 1600-5767

Volume 43| Part 5| October 2010| Pages 1078-1083

https://doi.org/10.1107/S0021889810027378

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