An account is given of the development of the SHELX system of computer programs from SHELX-76 to the present day. In addition to identifying useful innovations that have come into general use through their implementation in SHELX, a critical analysis is presented of the less-successful features, missed opportunities and desirable improvements for future releases of the software. An attempt is made to understand how a program originally designed for photographic intensity data, punched cards and computers over 10000 times slower than an average modern personal computer has managed to survive for so long. SHELXL is the most widely used program for small-molecule refinement and SHELXS and SHELXD are often employed for structure solution despite the availability of objectively superior programs. SHELXL also finds a niche for the refinement of macromolecules against high-resolution or twinned data; SHELXPRO acts as an interface for macromolecular applications. SHELXC, SHELXD and SHELXE are proving useful for the experimental phasing of macromolecules, especially because they are fast and robust and so are often employed in pipelines for high-throughput phasing. This paper could serve as a general literature citation when one or more of the open-source SHELX programs (and the Bruker AXS version SHELXTL) are employed in the course of a crystal-structure determination.

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A short history of SHELX

The improvements in the crystal structure refinement program SHELXL have been closely coupled with the development and increasing importance of the CIF (Crystallographic Information Framework) format for validating and archiving crystal structures. An important simplification is that now only one file in CIF format (for convenience, referred to simply as `a CIF') containing embedded reflection data and SHELXL instructions is needed for a complete structure archive; the program SHREDCIF can be used to extract the .hkl and .ins files required for further refinement with SHELXL. Recent developments in SHELXL facilitate refinement against neutron diffraction data, the treatment of H atoms, the determination of absolute structure, the input of partial structure factors and the refinement of twinned and disordered structures. SHELXL is available free to academics for the Windows, Linux and Mac OS X operating systems, and is particularly suitable for multiple-core processors.

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Crystal structure refinement with SHELXL

New software, OLEX2, has been developed for the determination, visualization and analysis of molecular crystal structures. The software has a portable mouse-driven workflow-oriented and fully comprehensive graphical user interface for structure solution, refinement and report generation, as well as novel tools for structure analysis. OLEX2 seamlessly links all aspects of the structure solution, refinement and publication process and presents them in a single workflow-driven package, with the ultimate goal of producing an application which will be useful to both chemists and crystallographers.

OLEX2: a complete structure solution, refinement and analysis program

抗原变异可使得多种致病微生物易于逃避宿主免疫应答。表达在感染红细胞表面的恶性疟原虫红细胞表面蛋白1（PfPMP1）与感染红细胞、内皮细胞、树突状细胞以及胎盘的单个或多个受体作用，在黏附及免疫逃避中起关键的作用。每个单倍体基因组var基因家族编码约60种成员，通过启动转录不同的var基因变异体为抗原变异提供了分子基础。

疟原虫var基因转换速率变化导致抗原变异[英]／Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A

Macromolecular X-ray crystallography is routinely applied to understand biological processes at a molecular level. How­ever, significant time and effort are still required to solve and complete many of these structures because of the need for manual interpretation of complex numerical data using many software packages and the repeated use of interactive three-dimensional graphics. PHENIX has been developed to provide a comprehensive system for macromolecular crystallo­graphic structure solution with an emphasis on the automation of all procedures. This has relied on the development of algorithms that minimize or eliminate subjective input, the development of algorithms that automate procedures that are traditionally performed by hand and, finally, the development of a framework that allows a tight integration between the algorithms.

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystals of the polar conformer of the quinoxaline antibiotic triostin A are orthorhombic, space group P212121, with a= 20.940(5), b= 18.528(4), and c= 18.795(4)A. There are two molecules of isoamyl acetate solvent per triostin A molecule. The cyclic octadepsipeptide has approximate two-fold symmetry. The quinoxaline chromophores and the disulphide cross-bridge project from opposite sides of the peptide ring. The conformation is compared with that found for the synthetic analogue TANDEM, and with the results of n.m.r. investigation. The observed structure accounts for the higher binding constants of the natural antibiotic, as well as its capacity to bind at GC-rich sequences in DNAs.

Crystal and molecular structure of the DNA-binding antitumour antibiotic triostin A

Balhimycin is a naturally occurring glycopeptide antibiotic, related to vancomycin which acts by binding nascent bacterial cell-wall peptide ending in the sequence d-Ala-d-Ala. Crystals of balhimycin are monoclinic, space group P21, a = 20.48 (10), b = 43.93 (21), c = 27.76 (14) A, β = 100.5 (5)° with four independent antibiotic molecules, three molecules of 2-methyl-2,4-pentanediol, two citrate ions, three acetate ions and 127.5 water molecules in the asymmetric unit. With an asymmetric unit larger than those of the smallest proteins and a solvent content of about 32%, the crystals have similar diffraction properties to those of small proteins. 27 387 unique reflections were collected using synchrotron radiation. The structure was solved by a standard protein technique, the molecular-replacement method, using ureido-balhimycin as search model. The anisotropic refinement against all F2 data between 0.96 and 45 A converged to a conventional R value of 11.27% with R1=\sum\big| |F_o|-|F_c| \big|/\sum|F_o| for the 24 623 data with I > 2σ(I) and 12.58% for all 27 387 data. The four monomers possess fairly similar conformations (r.m.s. deviation 0.7 A). Two antibiotic molecules form a tight dimer with antiparallel hydrogen bonds between the peptide backbone as well as between the vancosamine residues and the peptide backbone. In each of the two dimers, one binding pocket is occupied by a citrate ion and the other by an acetate ion. The dimer units are linked in the crystal by hydrogen bonds to form infinite chains.

Structure of Balhimycin and its Complex with Solvent Molecules

Cyclisation de methyl-7 octadiene-1,6dicarboxylates-1,1 de methyle en isopropenyl-2 cyclopentanemalonates de dimethyle

Induziert‐ und nicht‐induziert‐diastereoselektive intramolekulare En‐Reaktion von 1,6‐Dienen: Die ungewöhnliche Bildung von trans‐1,2‐disubstituierten Cyclopentanen

(Ph4P)2[CuCN(MoS4)] und (Me4N)2(CuCN)2MoS4: Thiomolybdat‐Liganden an Cu‐Atomen eines CuCN‐Moleküls und einer zickzack‐CuCN‐Kette

The linear phosphazene [H2NPPh2NPPh2NH2]Cl(1) reacts with MoCl3N and NbCl5 to form the new cyclometallaphosphazenes [graphic omitted]oCl3(3) and [graphic omitted]bCl2(4), respectively. The crystal structure of the acetonitrile adduct of the cyclomolybdaphosphazene (3) shows that the central six-membered ring is nearly planar.

George M. Sheldrick

Papers

Crystal and molecular structure of the DNA-binding antitumour antibiotic triostin A

Structure of Balhimycin and its Complex with Solvent Molecules

Induziert‐ und nicht‐induziert‐diastereoselektive intramolekulare En‐Reaktion von 1,6‐Dienen: Die ungewöhnliche Bildung von trans‐1,2‐disubstituierten Cyclopentanen

(Ph4P)2[CuCN(MoS4)] und (Me4N)2(CuCN)2MoS4: Thiomolybdat‐Liganden an Cu‐Atomen eines CuCN‐Moleküls und einer zickzack‐CuCN‐Kette

New heterocyclic compounds containing niobium and molybdenum; crystal structure of a cyclomolybdaphosphazene