Battery: eight more home-source sets (open arm), five small molecules (in-house arm)

Open arm, all IRRMC, single Cu K-alpha sweeps on Rigaku Saturn CCDs read
through the d*TREK SMV path: 3mc4 (H 3), 3meb (P 1 21 1, Saturn 944,
overflow ratio 32), 3p85 (P 63 2 2), 3r6o (I 41), 5uth (P 31 2 1), 5vml
(P 42 21 2), 6cee and 6v2r (P 21 21 21 / P 41 21 2, Saturn A200, unbinned
2048x2048, 0.1 mm pixels). Detector 2theta spans -10 to +10 deg. Run
20261002-1326_84228b_home-source-12: all pass except 3r6o, called I 4 2 2
against the deposited I 41 with twinning suspected (<|L|> 0.32). Two
further candidates (3r6h, 3sgw) were dropped: what the repository lists as
one dataset is two sweeps under one file template, split by a phi change,
which the reader refuses.

In-house arm: aspirin (20 and 25 keV), anhydrous citric acid, HEPES and YAG,
measured at X10SA. The reference is XDS's CORRECT.LP (refs --write) with
the space group taken from the literature as ref_override, because XDS
reports only Sohncke groups; each override cites its COD entry and paper.
Run 20261002-1354_84228b_small-molecules-inhouse: four pass, including
HEPES as P b c a where XDS has P 21 21 21; YAG is called I 41 3 2 against
I a -3 d (both programs merge it poorly, rugnux CC1/2 0.40, XDS ISa 3.2).

EXTERNAL_TEST_DATA.md gains the eight depositions (DOIs checked on DataCite)
and updated counts; the battery README lists the small-molecule standards
and has the current count of symlinked open-arm directories (42).

Co-Authored-By: Claude Opus 5.5 (1M context) <noreply@anthropic.com>

docs/EXTERNAL_TEST_DATA.md

@@ -4,7 +4,7 @@ Jungfraujoch is developed at the Swiss Light Source, but a data-reduction pipeli
 ever sees its own detectors is not tested. The datasets below were collected by other people,
 on detectors and in file formats we do not produce ourselves, and are used here to check that
 `rugnux` reads foreign files correctly and reduces them to sensible results. Most were collected
-at other facilities, two on laboratory X-ray sources; a few come from SLS beamlines, where the data are still written by someone
+at other facilities, ten on laboratory X-ray sources; a few come from SLS beamlines, where the data are still written by someone
 else's detector and someone else's acquisition system. Their authors published all of these for
 exactly this kind of reuse, and this page is where we credit them.
 
@@ -35,6 +35,10 @@ the table below; the repositories themselves are cited in
 | [36GK](https://www.rcsb.org/structure/36GK) | IRRMC [10.18430/M336GK](https://doi.org/10.18430/M336GK) | CLSI 08ID-1 | 2.28 | I 2 2 2 | 120.6 189.5 199.7 90.0 90.0 90.0 | Dectris Eiger 9M | D-GlcNAc-bound structure of Vibrio vulnificus putative carbohydrate binding module and split domain |
 | [3INP](https://www.rcsb.org/structure/3INP) | IRRMC [10.18430/m33inp](https://doi.org/10.18430/m33inp) | APS 21-ID-F | 2.05 | F 41 3 2 | 224.1 224.1 224.1 90.0 90.0 90.0 | marCCD, 225 mm plate | 2.05 Angstrom Resolution Crystal Structure of D-ribulose-phosphate 3-epimerase from Francisella tularensis. |
 | [3KY7](https://www.rcsb.org/structure/3KY7) | IRRMC [10.18430/m33ky7](https://doi.org/10.18430/m33ky7) | APS 21-ID-G | 2.35 | P 43 3 2 | 125.2 125.2 125.2 90.0 90.0 90.0 | marCCD, 300 mm plate | 2.35 Angstrom resolution crystal structure of a putative tRNA (guanine-7-)-methyltransferase (trmD) from Staphylococcus aureus subsp. aureus MRSA252 |
+| [3MC4](https://www.rcsb.org/structure/3MC4) | IRRMC [10.18430/M33MC4](https://doi.org/10.18430/M33MC4) | Home source, Rigaku MicroMax-007 HF | 1.95 | H 3 | 104.0 104.0 105.5 90.0 90.0 120.0 | Rigaku Saturn 944+ | Crystal structure of WW/RSP5/WWP domain: bacterial transferase hexapeptide repeat: serine O-Acetyltransferase from Brucella Melitensis |
+| [3MEB](https://www.rcsb.org/structure/3MEB) | IRRMC [10.18430/M33MEB](https://doi.org/10.18430/M33MEB) | Home source, Rigaku MicroMax-007 HF | 1.90 | P 1 21 1 | 58.6 101.2 81.5 90.0 90.6 90.0 | Rigaku Saturn 944 | Structure of cytoplasmic aspartate aminotransferase from giardia lamblia |
+| [3P85](https://www.rcsb.org/structure/3P85) | IRRMC [10.18430/M33P85](https://doi.org/10.18430/M33P85) | Home source, Rigaku FR-E+ SuperBright | 1.90 | P 63 2 2 | 127.3 127.3 72.9 90.0 90.0 120.0 | Rigaku Saturn 944+ | Crystal structure enoyl-coa hydratase from mycobacterium avium |
+| [3R6O](https://www.rcsb.org/structure/3R6O) | IRRMC [10.18430/M33R6O](https://doi.org/10.18430/M33R6O) | Home source, Rigaku FR-E+ SuperBright | 1.95 | I 41 | 90.7 90.7 76.1 90.0 90.0 90.0 | Rigaku Saturn 944+ | Crystal structure of a probable 2-hydroxyhepta-2,4-diene-1, 7-dioateisomerase from Mycobacterium abscessus |
 | [5CC8](https://www.rcsb.org/structure/5CC8) | IRRMC [10.18430/M35CC8](https://doi.org/10.18430/M35CC8) | Home source, Rigaku MicroMax-007 HF | 1.75 | P 21 21 2 | 87.1 93.8 72.5 90.0 90.0 90.0 | Rigaku Saturn 944+ | Structure of thiamine-monophosphate kinase from Acinetobacter baumannii in complex with AMPPNP |
 | [5EBI](https://www.rcsb.org/structure/5EBI) | MXRDR [10.18150/9887707](https://doi.org/10.18150/9887707) | BESSY 14.2 | 1.09 | P 1 21 1 | 35.7 44.1 35.7 90.0 120.0 90.0 | marCCD, 225 mm plate | Crystal structure of a DNA-RNA chimera in complex with Ba2+ ions: a case of unusual multi-domain twinning |
 | [5EPE](https://www.rcsb.org/structure/5EPE) | IRRMC [10.18430/m3159c](https://doi.org/10.18430/m3159c) | APS 21-ID-G | 1.90 | F 2 3 | 157.5 157.5 157.5 90.0 90.0 90.0 | Rayonix MX-300 | Crystal structure of SAM-dependent methyltransferase from Thiobacillus denitrificans in complex with S-Adenosyl-L-homocysteine |
@@ -49,7 +53,10 @@ the table below; the repositories themselves are cited in
 | [5REO](https://www.rcsb.org/structure/5REO) | Zenodo [10.5281/zenodo.3730956](https://doi.org/10.5281/zenodo.3730956) | Diamond I04-1 | 1.88 | C 1 2 1 | 112.4 52.6 44.4 90.0 103.0 90.0 | PILATUS 6M-F | PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102578 |
 | [5SRC](https://www.rcsb.org/structure/5SRC) | IRRMC [10.18430/M35SRC](https://doi.org/10.18430/M35SRC) | ALS 8.3.1 | 1.05 | P 43 | 88.7 88.7 39.2 90.0 90.0 90.0 | PILATUS3 6M | PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with Z5198562500 - (R,R) and (R,S) isomers |
 | [5T39](https://www.rcsb.org/structure/5T39) | SBGrid [10.15785/sbgrid/356](https://doi.org/10.15785/sbgrid/356) | APS 21-ID-F | 1.10 | P 1 21 1 | 50.2 41.3 58.5 90.0 98.6 90.0 | Rayonix MX-300 | Crystal Structure of the N-terminal domain of EvdMO1 in the presence of SAH and D-fucose |
+| [5UTH](https://www.rcsb.org/structure/5UTH) | IRRMC [10.18430/M35UTH](https://doi.org/10.18430/M35UTH) | Home source, Rigaku FR-E+ SuperBright | 1.95 | P 31 2 1 | 69.3 69.3 153.8 90.0 90.0 120.0 | Rigaku Saturn 944+ | Crystal structure of thioredoxin reductase from Mycobacterium smegmatis in complex with FAD |
+| [5VML](https://www.rcsb.org/structure/5VML) | IRRMC [10.18430/M35VML](https://doi.org/10.18430/M35VML) | Home source, Rigaku FR-E+ SuperBright | 1.70 | P 42 21 2 | 66.3 66.3 115.3 90.0 90.0 90.0 | Rigaku Saturn 944+ | Crystal Structure of Acetoacetyl-CoA Reductase from Burkholderia Pseudomallei 1710b with bound NADP |
 | [6CDL](https://www.rcsb.org/structure/6CDL) | IRRMC [10.18430/m36cdl](https://doi.org/10.18430/m36cdl) | APS 22-ID | 1.25 | P 21 21 2 | 58.3 85.9 46.1 90.0 90.0 90.0 | marCCD, 300 mm plate | HIV-1 wild type protease with GRL-03214A, 6-5-5-ring fused umbrella-like tetrahydropyranofuran as the P2-ligand, a cyclopropylaminobenzothiazole as the P2'-ligand and 3,5-difluorophenylmethyl as the P1-ligand |
+| [6CEE](https://www.rcsb.org/structure/6CEE) | IRRMC [10.18430/M36CEE](https://doi.org/10.18430/M36CEE) | Home source, Rigaku FR-E SuperBright | 1.55 | P 21 21 21 | 40.7 44.1 55.9 90.0 90.0 90.0 | Rigaku Saturn A200 | Crystal structure of fragment 3-(1-Methyl-2-oxo-1,2-dihydroquinoxalin-3-yl)propionic acid bound in the ubiquitin binding pocket of the HDAC6 zinc-finger domain |
 | [6F3P](https://www.rcsb.org/structure/6F3P) | IRRMC [10.18430/M36F3P](https://doi.org/10.18430/M36F3P) | APS 22-ID | 1.35 | C 1 2 1 | 142.9 85.7 112.0 90.0 122.2 90.0 | marCCD, 300 mm plate | Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa in complex with 3'-deoxyadenosine and K+ cation |
 | [6FID](https://www.rcsb.org/structure/6FID) | SBGrid [10.15785/sbgrid/541](https://doi.org/10.15785/sbgrid/541) | ESRF ID30B | 2.20 | P 21 21 21 | 59.9 64.1 69.7 90.0 90.0 90.0 | PILATUS3 6M | Bovine trypsin solved by S-SAD on ID30B |
 | [6FVZ](https://www.rcsb.org/structure/6FVZ) | IRRMC [10.18430/m36fvz](https://doi.org/10.18430/m36fvz) | ESRF ID23-2 | 1.80 | C 2 2 2 | 131.2 222.8 86.5 90.0 90.0 90.0 | PILATUS3 X 2M | Crystal structure of human monoamine oxidase B (MAO B) in complex with an inhibitor |
@@ -83,6 +90,7 @@ the table below; the repositories themselves are cited in
 | [6TTN](https://www.rcsb.org/structure/6TTN) | IRRMC [10.18430/m36ttn](https://doi.org/10.18430/m36ttn) | BESSY 14.1 | 1.12 | P 21 21 21 | 39.9 79.8 104.7 90.0 90.0 90.0 | PILATUS 6M | N-terminally truncated hyoscyamine 6-hydroxylase (tH6H) in complex with N-oxalylglycine and hyoscyamine |
 | [6U7G](https://www.rcsb.org/structure/6U7G) | IRRMC [10.18430/m36u7g](https://doi.org/10.18430/m36u7g) | APS 23-ID-B | 2.35 | P 1 21 1 | 99.6 98.7 147.5 90.0 104.6 90.0 | Dectris Eiger 16M | HCoV-229E RBD Class V in complex with human APN |
 | [6UKF](https://www.rcsb.org/structure/6UKF) | IRRMC [10.18430/m36ukf](https://doi.org/10.18430/m36ukf) | APS 22-ID | 1.00 | P 1 21 1 | 61.0 37.3 69.0 90.0 109.8 90.0 | Dectris Eiger 16M | HhaI endonuclease in Complex with DNA at 1 Angstrom Resolution |
+| [6V2R](https://www.rcsb.org/structure/6V2R) | IRRMC [10.18430/m36v2r](https://doi.org/10.18430/m36v2r) | Home source, Rigaku FR-E | 1.60 | P 41 21 2 | 40.2 40.2 83.1 90.0 90.0 90.0 | Rigaku Saturn A200 | Crystal Structure of chromodomain of CBX7 mutant V13A in complex with inhibitor UNC3866 |
 | [6VWW](https://www.rcsb.org/structure/6VWW) | IRRMC [10.18430/m36vww](https://doi.org/10.18430/m36vww) | APS 19-ID | 2.20 | P 63 | 150.5 150.5 111.3 90.0 90.0 120.0 | PILATUS3 6M | Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2. |
 | [6W4H](https://www.rcsb.org/structure/6W4H) | IRRMC [10.18430/m36w4h](https://doi.org/10.18430/m36w4h) | APS 21-ID-F | 1.80 | P 31 2 1 | 167.7 167.7 51.9 90.0 90.0 120.0 | Rayonix MX-300 | 1.80 Angstrom Resolution Crystal Structure of NSP16 - NSP10 Complex from SARS-CoV-2 |
 | [6W75](https://www.rcsb.org/structure/6W75) | IRRMC [10.18430/m36w75](https://doi.org/10.18430/m36w75) | APS 21-ID-F | 1.95 | P 32 2 1 | 166.2 166.2 98.3 90.0 90.0 120.0 | Rayonix MX-300 | 1.95 Angstrom Resolution Crystal Structure of NSP10 - NSP16 Complex from SARS-CoV-2 |
@@ -329,14 +337,14 @@ plate`), the comment's name where one is present (`Rayonix MX-300`), or the seri
 
 ## Deposited models and structure factors
 
-166 of the 173 datasets have a released PDB entry, and RCSB
+174 of the 181 datasets have a released PDB entry, and RCSB
 reports released structure factors (`status_code_sf = REL`) for every one of them. A merged
 result from this pipeline can therefore be checked against the deposited model or against the
 deposited intensities.
 
 ## Rows where our reduction and the deposition disagree
 
-Six of the 173 rows are ones where `rugnux` does not reproduce the deposited space group or
+Six of the 181 rows are ones where `rugnux` does not reproduce the deposited space group or
 cell, and where we have looked at the disagreement closely enough to change how the row is
 scored. They are collected here because a scoring row that silently disagrees with a published
 entry is not something a reader should have to discover from the code.
@@ -503,17 +511,17 @@ symmetries rather than to be easy to process. The counts below describe where it
 like everything else on this page, they are metadata about the depositions and their files, not
 measurements.
 
-- **Repository:** IRRMC 86, SBGrid 35, Zenodo 28, MXRDR 14, ESRF 3, Keele University 3, XRDa 3,
+- **Repository:** IRRMC 94, SBGrid 35, Zenodo 28, MXRDR 14, ESRF 3, Keele University 3, XRDa 3,
   UQ eSpace 1.
 - **Facility** - counted from the facility part of the Facility / beamline column, the beamline
   ignored so that entries deposited with and without one count the same, over the 170 rows that
   name one: APS 26, Diamond 20, ESRF 16, NSLS-II 14, BESSY 12, PETRA III 12, SSRL 11, ALS 8,
   SLS 7, SOLEIL 7, SPring-8 7, SSRF 6, PAL/PLS 5, CHESS 4, CLSI 3, ALBA 2, Australian
   Synchrotron 2, ELETTRA 2, LNLS 2, and one each from MAX IV, NSRRC, Photon Factory and RRCAT
-  Indus-2 - 23 facilities. The other two rows were collected on laboratory sources, a rotating
-  anode and a liquid-metal jet.
-- **Crystal system, from the deposited space group of the 166 PDB-coded rows:** orthorhombic 44,
-  monoclinic 40, tetragonal 22, trigonal 19, hexagonal 16, cubic 13, triclinic 12.
+  Indus-2 - 23 facilities. The other ten rows were collected on laboratory sources: nine on
+  rotating anodes and one on a liquid-metal jet.
+- **Crystal system, from the deposited space group of the 174 PDB-coded rows:** orthorhombic 45,
+  monoclinic 41, tetragonal 25, trigonal 21, hexagonal 17, cubic 13, triclinic 12.
 - **Long cell axes:** eleven PDB-coded rows have a deposited cell axis longer than 320 Å - 8V4O,
   9ZMU, 9Z72, 9YL4, 5NW5, 6QAJ, 7QIJ, 8T7R, 9H0Q, 6G1F and 6OEL.
 

tools/battery/README.md

@@ -15,7 +15,7 @@ run needed): `cd tools/battery && python3 test_score.py`.
 | arm | datasets | reference | manifest |
 |---|---|---|---|
 | **open** | public PDB depositions of raw diffraction data, plus a few published small-molecule sets | the deposited space group, cell and resolution | `open.json` (committed) |
-| **inhouse** | standard test crystals measured at the SLS (lysozyme, thaumatin, insulin, cytochrome C, myoglobin), plus no-crystal controls | XDS, from the `CORRECT.LP` beside each dataset | `inhouse.json` (committed) |
+| **inhouse** | standard test crystals measured at the SLS (lysozyme, thaumatin, insulin, cytochrome C, myoglobin), small-molecule standards (aspirin, citric acid, HEPES, YAG), plus no-crystal controls | XDS, from the `CORRECT.LP` beside each dataset; for the small molecules the space group is the literature's (`ref_override`), as XDS reports only Sohncke groups | `inhouse.json` (committed) |
 | **private** | user data | XDS, like inhouse | outside the repository; the local site config gives its path |
 
 Scoring checks these things in order, and the first one that fails decides the verdict: did it
@@ -138,7 +138,7 @@ the copies. The paths inside the manifests do not change.
   [`docs/EXTERNAL_TEST_DATA.md`](../../docs/EXTERNAL_TEST_DATA.md). The sources are IRRMC
   (proteindiffraction.org), SBGrid Data Bank, Zenodo and a few others, and the page also says what
   each archive holds. Please cite those DOIs. At PSI the data root is `/home/data/open`, a
-  symlink to `/home/data/nonsls/raw`. 69 of the dataset directories in it are themselves symlinks
+  symlink to `/home/data/nonsls/raw`. 42 of the dataset directories in it are themselves symlinks
   into `/data/scout_staging2`, so **copy with symlinks followed**: `rsync -aL` or `cp -rL`.
   A plain `rsync -a` copies dangling links. The open arm is about 1.7 TB.
 - **inhouse**: these are our own measurements and cannot be downloaded publicly. Ask the

tools/battery/inhouse.json

@@ -37,5 +37,10 @@
  {"id": "myob_x06da_split", "input": "myob_x06da_split/MyoB2-4_079740_master.h5", "ref": {"sgno": 3, "cell": [35.39, 28.783, 63.626, 90.0, 105.544, 90.0], "anomalous": false, "isa": 12.41, "completeness": 77.7, "r_meas": 0.577, "cc_half": 0.984, "multiplicity": 4.38, "dmin_low": 4.48, "r_meas_low": 0.091, "dmin": 1.506, "dmin_rule": "xds_range", "dmin_xds": 1.506, "dmax": 50.0}, "tags": ["h5", "myoglobin", "twin"]},
  {"id": "myob_x06da_sparse", "input": "myob_x06da_sparse/MyoB2-5_7cef9c_master.h5", "ref": {"sgno": 3, "cell": [35.388, 28.752, 64.083, 90.0, 106.352, 90.0], "anomalous": false, "isa": 5.46, "completeness": 73.7, "r_meas": 0.326, "cc_half": 0.972, "multiplicity": 5.21, "dmin_low": 5.92, "r_meas_low": 0.146, "dmin": 2.0, "dmin_rule": "xds_range", "dmin_xds": 2.0, "dmax": 50.0}, "tags": ["h5", "myoglobin", "twin"]},
  {"id": "nothing_2", "input": "nothing_2/test-28_3400ac_master.h5", "expect": "no_lattice", "tags": ["h5", "control"]},
- {"id": "nothing_1", "input": "nothing_1/test-28_9bf604_master.h5", "expect": "no_lattice", "tags": ["h5", "control"]}
+ {"id": "nothing_1", "input": "nothing_1/test-28_9bf604_master.h5", "expect": "no_lattice", "tags": ["h5", "control"]},
+ {"id": "aspirin_x10sa_20keV", "input": "aspirin_x10sa_20keV/aspirin_1_002_master.h5", "tags": ["h5", "monoclinic", "small-molecule"], "ref": {"sgno": 4, "cell": [11.262, 6.543, 11.257, 90.0, 95.916, 90.0], "anomalous": true, "isa": 27.97, "completeness": 84.0, "r_meas": 0.032, "cc_half": 0.999, "multiplicity": 3.14, "dmin_low": 2.01, "r_meas_low": 0.03, "dmin": 0.68, "dmin_rule": "xds_range", "dmin_xds": 0.68, "dmax": 50.0}, "ref_override": {"sg": "P 1 21/c 1", "sgno": 14}, "ref_override_why": "aspirin form I, P 21/c; COD 7050897 - C. C. Wilson, New J. Chem. 26 (2002) 1733-1739, doi:10.1039/b203775k. XDS reports only Sohncke groups (P 21)"},
+ {"id": "aspirin_x10sa_25keV", "input": "aspirin_x10sa_25keV/aspirin_1_001_master.h5", "tags": ["h5", "monoclinic", "small-molecule"], "ref": {"sgno": 4, "cell": [11.255, 6.541, 11.259, 90.0, 95.916, 90.0], "anomalous": true, "isa": 29.55, "completeness": 86.6, "r_meas": 0.033, "cc_half": 0.999, "multiplicity": 3.15, "dmin_low": 1.63, "r_meas_low": 0.03, "dmin": 0.55, "dmin_rule": "xds_range", "dmin_xds": 0.55, "dmax": 50.0}, "ref_override": {"sg": "P 1 21/c 1", "sgno": 14}, "ref_override_why": "aspirin form I, P 21/c; COD 7050897 - C. C. Wilson, New J. Chem. 26 (2002) 1733-1739, doi:10.1039/b203775k. XDS reports only Sohncke groups (P 21)"},
+ {"id": "citricacid_x10sa_20keV", "input": "citricacid_x10sa_20keV/citricacid_1_005_master.h5", "tags": ["h5", "monoclinic", "small-molecule"], "ref": {"sgno": 4, "cell": [11.454, 5.579, 12.67, 90.0, 111.587, 90.0], "anomalous": true, "isa": 20.55, "completeness": 81.0, "r_meas": 0.04, "cc_half": 0.997, "multiplicity": 3.1, "dmin_low": 2.02, "r_meas_low": 0.043, "dmin": 0.68, "dmin_rule": "xds_range", "dmin_xds": 0.68, "dmax": 50.0}, "ref_override": {"sg": "P 1 21/c 1", "sgno": 14}, "ref_override_why": "anhydrous citric acid, P 21/a (P 21/c in the standard setting); COD 5000063 - J. P. Glusker, J. A. Minkin, A. L. Patterson, Acta Cryst. B25 (1969) 1066-1072, doi:10.1107/S0567740869003542. XDS reports only Sohncke groups (P 21)"},
+ {"id": "hepes_x10sa_20keV", "input": "hepes_x10sa_20keV/hepes_1_004_master.h5", "tags": ["h5", "orthorhombic", "small-molecule"], "ref": {"sgno": 19, "cell": [8.348, 9.575, 27.068, 90.0, 90.0, 90.0], "anomalous": true, "isa": 28.39, "completeness": 91.6, "r_meas": 0.03, "cc_half": 0.999, "multiplicity": 5.64, "dmin_low": 2.0, "r_meas_low": 0.035, "dmin": 0.68, "dmin_rule": "xds_range", "dmin_xds": 0.68, "dmax": 50.0}, "ref_override": {"sg": "P b c a", "sgno": 61}, "ref_override_why": "HEPES, P b c a; COD 2224210 (100 K, 8.341 9.567 27.066) - P. Sledz, T. Minor, M. Chruszcz, Acta Cryst. E65 (2009) o3027-o3028, doi:10.1107/S1600536809042512. XDS reports only Sohncke groups (P 21 21 21)"},
+ {"id": "yag_x10sa_20keV", "input": "yag_x10sa_20keV/yag_2_004_master.h5", "tags": ["h5", "cubic", "small-molecule"], "ref": {"sgno": 211, "cell": [11.997, 11.997, 11.997, 90.0, 90.0, 90.0], "anomalous": true, "isa": 3.2, "completeness": 99.0, "r_meas": 0.425, "cc_half": 0.958, "multiplicity": 27.96, "dmin_low": 1.99, "r_meas_low": 0.447, "dmin": 0.68, "dmin_rule": "xds_range", "dmin_xds": 0.68, "dmax": 50.0}, "ref_override": {"sg": "I a -3 d", "sgno": 230}, "ref_override_why": "Y3Al5O12 garnet, I a -3 d; COD 2003066 - A. Nakatsuka, A. Yoshiasa, T. Yamanaka, Acta Cryst. B55 (1999) 266-272, doi:10.1107/S0108768198012567. XDS reports only Sohncke groups (I 4 3 2)"}
 ]}

tools/battery/open.json

@@ -3,6 +3,10 @@
  {"id": "36gk", "input": "36gk/CLS-0074_5-3_36GK/data/CLS-0074_5-3_master.h5", "ref": {"sg": "I 2 2 2", "sgno": 23, "cell": [120.58, 189.49, 199.69, 90.0, 90.0, 90.0], "dmin": 2.28}, "tags": ["h5", "orthorhombic"]},
  {"id": "3inp", "input": "3inp/IDP02542_3inp/data/idp02542b.001", "ref": {"sg": "F 41 3 2", "sgno": 210, "cell": [224.08, 224.08, 224.08, 90.0, 90.0, 90.0], "dmin": 2.05}, "tags": ["marCCD", "cubic"]},
  {"id": "3ky7", "input": "3ky7/IDP90258_3ky7/data/idp90258f.001", "ref": {"sg": "P 43 3 2", "sgno": 212, "cell": [125.176, 125.176, 125.176, 90.0, 90.0, 90.0], "dmin": 2.35}, "tags": ["marCCD", "cubic"]},
+ {"id": "3mc4", "input": "3mc4/series/206918e4_x0001.img", "ref": {"sg": "H 3", "sgno": 146, "cell": [104.03, 104.03, 105.54, 90.0, 90.0, 120.0], "dmin": 1.95}, "tags": ["smv", "trigonal", "home-source"]},
+ {"id": "3meb", "input": "3meb/series/202097g3_x0001.img", "ref": {"sg": "P 1 21 1", "sgno": 4, "cell": [58.58, 101.15, 81.53, 90.0, 90.62, 90.0], "dmin": 1.9}, "tags": ["smv", "monoclinic", "home-source"]},
+ {"id": "3p85", "input": "3p85/series/217175d10_x0001.img", "ref": {"sg": "P 63 2 2", "sgno": 182, "cell": [127.29, 127.29, 72.9, 90.0, 90.0, 120.0], "dmin": 1.9}, "tags": ["smv", "hexagonal", "home-source"]},
+ {"id": "3r6o", "input": "3r6o/series/219594b8_x0001.img", "ref": {"sg": "I 41", "sgno": 80, "cell": [90.68, 90.68, 76.13, 90.0, 90.0, 90.0], "dmin": 1.95}, "tags": ["smv", "tetragonal", "home-source"]},
  {"id": "5cc8", "input": "5cc8/data/263060g10_x0001.img", "ref": {"sg": "P 21 21 2", "sgno": 18, "cell": [87.14, 93.76, 72.49, 90.0, 90.0, 90.0], "dmin": 1.75}, "tags": ["smv", "orthorhombic", "home-source", "tncs"]},
  {"id": "5ebi", "input": "5ebi/dna-rna-chimera_Ba_high_2_001.img", "ref": {"sg": "P 1 21 1", "sgno": 4, "cell": [35.72, 44.1, 35.72, 90.0, 119.98, 90.0], "dmin": 1.09}, "pinned": true, "tags": ["marCCD", "monoclinic", "twin"]},
  {"id": "5epe", "input": "5epe/030805_5epe/data/E1_7_set.001", "ref": {"sg": "F 2 3", "sgno": 196, "cell": [157.536, 157.536, 157.536, 90.0, 90.0, 90.0], "dmin": 1.9}, "tags": ["marCCD", "cubic"]},
@@ -14,6 +18,9 @@
  {"id": "5nw5", "input": "5nw5/5NW5_1_00001.cbf", "ref": {"sg": "P 21 21 21", "sgno": 19, "cell": [92.14, 169.8, 390.16, 90.0, 90.0, 90.0], "dmin": 6.502}, "tags": ["cbf", "orthorhombic", "low-resolution"]},
  {"id": "5reo", "input": "5reo/cbf/Mpro-x0752_1_0001.cbf", "ref": {"sg": "C 1 2 1", "sgno": 5, "cell": [112.39, 52.59, 44.38, 90.0, 103.04, 90.0], "dmin": 1.88}, "tags": ["cbf", "monoclinic"], "tiers": {"smoke": "fastest set (10 s): miniCBF, monoclinic"}},
  {"id": "5src", "input": "5src/5src/data/FRS004_15_1_00001.cbf", "ref": {"sg": "P 43", "sgno": 78, "cell": [88.68, 88.68, 39.23, 90.0, 90.0, 90.0], "dmin": 1.05}, "tags": ["cbf", "tetragonal"]},
+ {"id": "5uth", "input": "5uth/data/287007e1_0001.img", "ref": {"sg": "P 31 2 1", "sgno": 152, "cell": [69.28, 69.28, 153.8, 90.0, 90.0, 120.0], "dmin": 1.95}, "tags": ["smv", "trigonal", "home-source"]},
+ {"id": "5vml", "input": "5vml/data/271705c8_x_0001.img", "ref": {"sg": "P 42 21 2", "sgno": 94, "cell": [66.31, 66.31, 115.26, 90.0, 90.0, 90.0], "dmin": 1.7}, "tags": ["smv", "tetragonal", "home-source"]},
+ {"id": "6cee", "input": "6cee/data/Rachel_AV6_screen_0001.img", "ref": {"sg": "P 21 21 21", "sgno": 19, "cell": [40.72, 44.11, 55.91, 90.0, 90.0, 90.0], "dmin": 1.55}, "tags": ["smv", "orthorhombic", "home-source"]},
  {"id": "6fid", "input": "6fid/Trypsin_x1_align_2_0001.cbf", "ref": {"sg": "P 21 21 21", "sgno": 19, "cell": [59.947, 64.107, 69.694, 90.0, 90.0, 90.0], "dmin": 2.2}, "tags": ["cbf", "orthorhombic"]},
  {"id": "6fvz", "input": "6fvz/maox215_6fvz/data/maox215_w1_1_0001.cbf", "ref": {"sg": "C 2 2 2", "sgno": 21, "cell": [131.182, 222.753, 86.482, 90.0, 90.0, 90.0], "dmin": 1.8}, "tags": ["cbf", "orthorhombic"]},
  {"id": "6fwc", "input": "6fwc/maox225_6fwc/data/maox225_1_00001.cbf", "ref": {"sg": "C 2 2 2", "sgno": 21, "cell": [131.728, 222.051, 86.293, 90.0, 90.0, 90.0], "dmin": 1.7}, "tags": ["cbf", "orthorhombic"]},
@@ -42,6 +49,7 @@
  {"id": "6ttn", "input": "6ttn/6ttn/data/H6H_33_01_hyo_full_1_0001.cbf", "ref": {"sg": "P 21 21 21", "sgno": 19, "cell": [39.894, 79.841, 104.701, 90.0, 90.0, 90.0], "dmin": 1.12}, "tags": ["cbf", "orthorhombic"]},
  {"id": "6u7g", "input": "6u7g/6u7g/data/SNB02_11_8_1_master.h5", "ref": {"sg": "P 1 21 1", "sgno": 4, "cell": [99.555, 98.682, 147.525, 90.0, 104.6, 90.0], "dmin": 2.35}, "pinned": true, "tags": ["h5", "monoclinic"]},
  {"id": "6ukf", "input": "6ukf/6ukf/data/XDC-7_Pn6_000001.cbf", "ref": {"sg": "P 1 21 1", "sgno": 4, "cell": [61.018, 37.317, 69.027, 90.0, 109.768, 90.0], "dmin": 1.0}, "tags": ["cbf", "monoclinic"]},
+ {"id": "6v2r", "input": "6v2r/data/cbx7.248483.hv6_screen_0001.img", "ref": {"sg": "P 41 21 2", "sgno": 92, "cell": [40.193, 40.193, 83.127, 90.0, 90.0, 90.0], "dmin": 1.6}, "tags": ["smv", "tetragonal", "home-source"]},
  {"id": "6vww", "input": "6vww/IDP51000_6vww/data/m4H11g_00001.cbf", "ref": {"sg": "P 63", "sgno": 173, "cell": [150.539, 150.539, 111.31, 90.0, 90.0, 120.0], "dmin": 2.2}, "tags": ["cbf", "hexagonal", "twin"], "tiers": {"smoke": "merohedral twin, P63"}},
  {"id": "6w4h", "input": "6w4h/IDP51000_6W4H/data/idp51000-201-a_1_2_3.001", "ref": {"sg": "P 31 2 1", "sgno": 152, "cell": [167.74, 167.74, 51.942, 90.0, 90.0, 120.0], "dmin": 1.8}, "tags": ["marCCD", "trigonal"]},
  {"id": "6wzo", "input": "6wzo/9_1_1_000001.cbf", "ref": {"sg": "P 1", "sgno": 1, "cell": [43.718, 50.061, 69.337, 106.499, 90.094, 97.145], "dmin": 1.42}, "tags": ["cbf", "triclinic"]},