2JIC

High resolution structure of xylanase-II from one micron beam experiment

Summary for 2JIC

• Entry DOI: 10.2210/pdb2jic/pdb
• Descriptor: XYLANASE-II (2 entities in total)
• Functional Keywords: hydrolase, endonuclease, xylan degradation, fungi, xylan, microbeam, glycosidase
• Biological source: TRICHODERMA LONGIBRACHIATUM
• Total number of polymer chains: 1
• Total formula weight: 20858.53

Authors

Moukhametzianov, R.,Burghammer, M.,Edwards, P.C.,Petitdemange, S.,Popov, D.,Fransen, M.,Schertler, G.F.,Riekel, C. (deposition date: 2007-02-27, release date: 2008-05-13, Last modification date: 2023-12-13)

Primary citation

Moukhametzianov, R.,Burghammer, M.,Edwards, P.C.,Petitdemange, S.,Popov, D.,Fransen, M.,Mcmullan, G.,Schertler, G.F.,Riekel, C.
Protein Crystallography with a Micrometre-Sized Synchrotron-Radiation Beam.
Acta Crystallogr.,Sect.D, 64:158-, 2008

PubMed Abstract: For the first time, protein microcrystallography has been performed with a focused synchrotron-radiation beam of 1 microm using a goniometer with a sub-micrometre sphere of confusion. The crystal structure of xylanase II has been determined with a flux density of about 3 x 10(10) photons s(-1) microm(-2) at the sample. Two sets of diffraction images collected from different sized crystals were shown to comprise data of good quality, which allowed a 1.5 A resolution xylanase II structure to be obtained. The main conclusion of this experiment is that a high-resolution diffraction pattern can be obtained from 20 microm(3) crystal volume, corresponding to about 2 x 10(8) unit cells. Despite the high irradiation dose in this case, it was possible to obtain an excellent high-resolution map and it could be concluded from the individual atomic B-factor patterns that there was no evidence of significant radiation damage. The photoelectron escape from a narrow diffraction channel is a possible reason for reduced radiation damage as indicated by Monte Carlo simulations. These results open many new opportunities in scanning protein microcrystallography and make random data collection from microcrystals a real possibility, therefore enabling structures to be solved from much smaller crystals than previously anticipated as long as the crystallites are well ordered.

PubMed: 18219115
DOI: 10.1107/S090744490705812X

Experimental method

X-RAY DIFFRACTION (1.5 Å)